6GPL

Crystal structure of human GDP-D-mannose 4,6-dehydratase in complex with GDP-4k6d-Man

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth B]	d6gplb_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	GDP-mannose 4,6-dehydratase	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B [auth C]	d6gplc_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	GDP-mannose 4,6-dehydratase	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C [auth D]	d6gpld_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	GDP-mannose 4,6-dehydratase	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D [auth E]	d6gple_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	GDP-mannose 4,6-dehydratase	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth B]	SCOP2B Superfamily	SDR-like	8058507	3000038	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	SDR-like	8058507	3000038	SCOP2B (2022-06-29)
C [auth D]	SCOP2B Superfamily	SDR-like	8058507	3000038	SCOP2B (2022-06-29)
D [auth E]	SCOP2B Superfamily	SDR-like	8058507	3000038	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)
A [auth B]	GDP_Man_Dehyd	e6gplB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)
B [auth C]	GDP_Man_Dehyd	e6gplC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)
C [auth D]	GDP_Man_Dehyd	e6gplD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)
D [auth E]	GDP_Man_Dehyd	e6gplE1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A [auth B]	3.90.25.10	Alpha Beta	Alpha-Beta Complex	UDP-galactose 4-epimerase	domain 1	CATH (4.3.0)
B [auth C]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B [auth C]	3.90.25.10	Alpha Beta	Alpha-Beta Complex	UDP-galactose 4-epimerase	domain 1	CATH (4.3.0)
C [auth D]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C [auth D]	3.90.25.10	Alpha Beta	Alpha-Beta Complex	UDP-galactose 4-epimerase	domain 1	CATH (4.3.0)
D [auth E]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
D [auth E]	3.90.25.10	Alpha Beta	Alpha-Beta Complex	UDP-galactose 4-epimerase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth C], C [auth D], D [auth E]	PF16363	GDP-mannose 4,6 dehydratase (GDP_Man_Dehyd)	GDP-mannose 4,6 dehydratase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth C], C [auth D], D [auth E]	GDP-mannose 4,6 dehydratase	NADP+ binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding NADP binding small molecule binding GDP-mannose 4,6-dehydratase activity hydro-lyase activity NADP+ binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding NADP binding small molecule binding GDP-mannose 4,6-dehydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity identical protein binding protein binding	cellular response to stimulus regulation of biological process regulation of cellular process cell surface receptor signaling pathway response to stimulus signaling biological regulation cell communication Notch signaling pathway cellular process signal transduction nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process nucleotide-sugar metabolic process cellular response to stimulus regulation of biological process regulation of cellular process cell surface receptor signaling pathway response to stimulus signaling biological regulation cell communication Notch signaling pathway cellular process signal transduction nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process small molecule metabolic process metabolic process primary metabolic process GDP-mannose metabolic process carbohydrate derivative biosynthetic process cellular metabolic process 'de novo' GDP-L-fucose biosynthetic process GDP-L-fucose metabolic process nucleobase-containing compound biosynthetic process biosynthetic process nucleotide-sugar biosynthetic process phosphorus metabolic process GDP-L-fucose biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth C], C [auth D], D [auth E]	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A [auth B], B [auth C], C [auth D], D [auth E]	IPR016040	NAD(P)-binding domain	Domain
A [auth B], B [auth C], C [auth D], D [auth E]	IPR006368	GDP-mannose 4,6-dehydratase	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth B], B [auth C], C [auth D], D [auth E]	Pharos: O60547	ulcerative colitis astrocytic tumor ductal breast carcinoma in situ lung cancer nasopharyngeal carcinoma ovarian cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia spina bifida brachydactyly type E1 heart disease lung carcinoma non-small cell lung carcinoma pancreatic intraductal papillary-mucinous carcinoma plasma cell myeloma tuberculosis ulcerative colitis astrocytic tumor ductal breast carcinoma in situ lung cancer nasopharyngeal carcinoma ovarian cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia spina bifida brachydactyly type E1 heart disease lung carcinoma non-small cell lung carcinoma pancreatic intraductal papillary-mucinous carcinoma plasma cell myeloma tuberculosis Crohn disease lung adenocarcinoma medulloblastoma open-angle glaucoma pancreatic intraductal papillary-mucinous neoplasm psoriasis

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 R01GM133198.