6IHC

Crystal structure of (3R)-Hydroxyacyl-Acyl Carrier Protein Dehydratase(FabZ) Y100A mutant in complex with holo-ACP from Helicobacter pylori

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
G	d6ihcg_	All alpha proteins	Acyl carrier protein-like	ACP-like	automated matches	automated matches	(Helicobacter pylori ) [TaxId: 210 ],	SCOPe (2.08)
A	d6ihca_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	Campylobacter pylori (Helicobacter pylori ) [TaxId: 210 ],	SCOPe (2.08)
B	d6ihcb_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	Campylobacter pylori (Helicobacter pylori ) [TaxId: 210 ],	SCOPe (2.08)
C	d6ihcc_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	Campylobacter pylori (Helicobacter pylori ) [TaxId: 210 ],	SCOPe (2.08)
D	d6ihcd_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	Campylobacter pylori (Helicobacter pylori ) [TaxId: 210 ],	SCOPe (2.08)
E	d6ihce_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	Campylobacter pylori (Helicobacter pylori ) [TaxId: 210 ],	SCOPe (2.08)
F	d6ihcf_	Alpha and beta proteins (a+b)	Thioesterase/thiol ester dehydrase-isomerase	Thioesterase/thiol ester dehydrase-isomerase	FabZ-like	(3R)-hydroxymyristoyl ACP dehydrase FabZ	Campylobacter pylori (Helicobacter pylori ) [TaxId: 210 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
G	SCOP2B Superfamily	ACP-like	8074630	3001805	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8088180	3000149	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8088180	3000149	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8088180	3000149	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8088180	3000149	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8088180	3000149	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8088180	3000149	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
G	PP-binding	e6ihcG1	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PP-binding	ECOD (1.6)
A	FabA	e6ihcA1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
B	FabA	e6ihcB1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
C	FabA	e6ihcC1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
D	FabA	e6ihcD1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
E	FabA	e6ihcE1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)
F	FabA	e6ihcF1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: FabA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (utative)
B	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (utative)
C	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (utative)
D	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (utative)
E	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (utative)
F	3.10.129.10	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
G	PF00550	Phosphopantetheine attachment site (PP-binding)	Phosphopantetheine attachment site	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.	Domain
A, B, C, D, E A, B, C, D, E, F	PF07977	FabA-like domain (FabA)	FabA-like domain	This enzyme domain has a HotDog fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
G	holo-form acyl carrier protein (holo-ACP)	phosphopantetheine-dependent carrier activity prosthetic group binding binding acyl carrier activity molecular carrier activity ACP phosphopantetheine attachment site binding acyl binding small molecule binding vitamin binding amide binding modified amino acid binding phosphopantetheine binding	glycolipid metabolic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process liposaccharide metabolic process primary metabolic process glycolipid biosynthetic process glycolipid metabolic process lipid A biosynthetic process carbohydrate derivative metabolic process lipid biosynthetic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process liposaccharide metabolic process primary metabolic process glycolipid biosynthetic process phospholipid biosynthetic process lipid A metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process metabolic process cellular process membrane lipid biosynthetic process lipid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol
A, B, C, D, E A, B, C, D, E, F	3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ	(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process glycolipid metabolic process lipid A biosynthetic process carbohydrate derivative metabolic process phospholipid metabolic process phosphate-containing compound metabolic process lipooligosaccharide biosynthetic process phosphorus metabolic process carbohydrate derivative biosynthetic process membrane lipid metabolic process lipooligosaccharide metabolic process liposaccharide metabolic process glycolipid biosynthetic process phospholipid biosynthetic process lipid A metabolic process organophosphate metabolic process organophosphate biosynthetic process membrane lipid biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
G	IPR006162	Phosphopantetheine attachment site	PTM
G	IPR020806	Polyketide synthase, phosphopantetheine-binding domain	Domain
G	IPR009081	Phosphopantetheine binding ACP domain	Domain
G	IPR036736	ACP-like superfamily	Homologous Superfamily
G	IPR003231	Acyl carrier protein	Family
A, B, C, D, E A, B, C, D, E, F	IPR010084	Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ	Family
A, B, C, D, E A, B, C, D, E, F	IPR013114	Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ	Family
A, B, C, D, E A, B, C, D, E, F	IPR029069	HotDog domain superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.