4QJG

Structure of a putative peptidoglycan glycosyltransferase from Atopobium parvulum in complex with penicillin V

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PBP_dimer_2	e4qjgA2	A: beta complex topology	X: Penicillin binding protein dimerisation domain (From Topology)	H: Penicillin binding protein dimerisation domain (From Topology)	T: Penicillin binding protein dimerisation domain	F: PBP_dimer_2	ECOD (1.6)
A	Transpeptidase_1st_1	e4qjgA3	A: alpha complex topology	X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins	F: Transpeptidase_1st_1	ECOD (1.6)
A	Transpeptidase_2nd	e4qjgA1	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Transpeptidase_2nd	ECOD (1.6)
B	PBP_dimer_2	e4qjgB1	A: beta complex topology	X: Penicillin binding protein dimerisation domain (From Topology)	H: Penicillin binding protein dimerisation domain (From Topology)	T: Penicillin binding protein dimerisation domain	F: PBP_dimer_2	ECOD (1.6)
B	Transpeptidase_1st_1	e4qjgB3	A: alpha complex topology	X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins	F: Transpeptidase_1st_1	ECOD (1.6)
B	Transpeptidase_2nd	e4qjgB2	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Transpeptidase_2nd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1310.10	Alpha Beta	Alpha-Beta Complex	Penicillin-binding protein 2a (Domain 2)	Penicillin-binding protein 2a (Domain 2)	CATH (4.3.0)
A	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
B	3.90.1310.10	Alpha Beta	Alpha-Beta Complex	Penicillin-binding protein 2a (Domain 2)	Penicillin-binding protein 2a (Domain 2)	CATH (4.3.0)
B	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00905	Penicillin binding protein transpeptidase domain (Transpeptidase)	Penicillin binding protein transpeptidase domain	The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.	Domain
A, B	PF21922	Penicillin binding protein A dimerisation domain (PBP_dimer_2)	Penicillin binding protein A dimerisation domain	This domain is found in peptidoglycan D,D-transpeptidase also known as penicillin-binding protein A (PBPA). This domain consists of a four-stranded mixed beta-sheet with three short helices packed on one side [2]. Compared to the N-terminal domains o ...	This domain is found in peptidoglycan D,D-transpeptidase also known as penicillin-binding protein A (PBPA). This domain consists of a four-stranded mixed beta-sheet with three short helices packed on one side [2]. Compared to the N-terminal domains of other class B High Molecular Mass (HMM) PBPs, the NTD of PBPA is relatively small because it contains only the so-called inter-domain linker region [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Peptidoglycan glycosyltransferase	glycosyltransferase activity transferase activity catalytic activity carbohydrate derivative transmembrane transporter activity macromolecule transmembrane transporter activity peptidoglycan transmembrane transporter activity lipid-linked peptidoglycan transporter activity transporter activity transmembrane transporter activity amide binding organic acid binding binding ion binding organic cyclic compound binding glycosyltransferase activity transferase activity catalytic activity carbohydrate derivative transmembrane transporter activity macromolecule transmembrane transporter activity peptidoglycan transmembrane transporter activity lipid-linked peptidoglycan transporter activity transporter activity transmembrane transporter activity amide binding organic acid binding binding ion binding organic cyclic compound binding anion binding penicillin binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding	developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis cellular process cell division	cell division site cellular anatomical entity membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001182	Probable peptidoglycan glycosyltransferase FtsW/RodA	Family
A, B	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
A, B	IPR054120	Penicillin binding protein A, dimerisation domain	Domain
A, B	IPR001460	Penicillin-binding protein, transpeptidase	Domain
A, B	IPR036138	Penicillin-binding protein, dimerisation 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.