Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2CZC

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Pyrococcus horikoshii OT3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A	0005737	cellular_component	cytoplasm
A	0006096	biological_process	glycolytic process
A	0008839	molecular_function	4-hydroxy-tetrahydrodipicolinate reductase
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0043891	molecular_function	glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity
A	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B	0005737	cellular_component	cytoplasm
B	0006096	biological_process	glycolytic process
B	0008839	molecular_function	4-hydroxy-tetrahydrodipicolinate reductase
B	0009089	biological_process	lysine biosynthetic process via diaminopimelate
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0043891	molecular_function	glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity
B	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
C	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C	0005737	cellular_component	cytoplasm
C	0006096	biological_process	glycolytic process
C	0008839	molecular_function	4-hydroxy-tetrahydrodipicolinate reductase
C	0009089	biological_process	lysine biosynthetic process via diaminopimelate
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0043891	molecular_function	glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity
C	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D	0005737	cellular_component	cytoplasm
D	0006096	biological_process	glycolytic process
D	0008839	molecular_function	4-hydroxy-tetrahydrodipicolinate reductase
D	0009089	biological_process	lysine biosynthetic process via diaminopimelate
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0043891	molecular_function	glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity
D	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 601

Chain	Residue
A	SER140
A	CYS141
A	ASN142
A	ARG166
A	HIS191
A	HIS192
A	HOH644
A	HOH746

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 602

Chain	Residue
A	ARG167
A	ALA168
A	ARG176
A	HOH737
A	ARG166

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 603

Chain	Residue
B	SER140
B	CYS141
B	ASN142
B	ARG166
B	HIS191
B	HIS192
B	HOH691

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 C 604

Chain	Residue
C	SER140
C	CYS141
C	ASN142
C	ARG166
C	HIS191
C	HIS192
C	HOH679
C	HOH681
C	HOH703

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 605

Chain	Residue
D	SER140
D	CYS141
D	ASN142
D	HIS191
D	HIS192
D	HOH653

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD A 501

Chain	Residue
A	ASN8
A	TYR10
A	GLY11
A	THR12
A	ILE13
A	THR35
A	ALA54
A	ALA86
A	THR87
A	PRO88
A	GLN109
A	GLY111
A	CYS141
A	ARG167
A	ASP170
A	GLN298
A	HOH614
A	HOH621
A	HOH625
A	HOH682
A	HOH747
A	HOH749

site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD B 502

Chain	Residue
B	ASN8
B	GLY9
B	TYR10
B	GLY11
B	THR12
B	ILE13
B	THR35
B	ALA54
B	ALA86
B	THR87
B	PRO88
B	GLN109
B	GLY111
B	CYS141
B	ARG167
B	ASP170
B	GLN298
B	HOH617
B	HOH640
B	HOH650
B	HOH672
B	HOH726
B	HOH728

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD C 503

Chain	Residue
C	HOH715
C	HOH716
C	ASN8
C	GLY9
C	TYR10
C	GLY11
C	THR12
C	ILE13
C	ALA86
C	THR87
C	GLN109
C	GLY111
C	CYS141
C	ARG167
C	ASP170
C	GLN298
C	HOH613
C	HOH643
C	HOH679
C	HOH710
C	HOH714

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD D 504

Chain	Residue
D	ASN8
D	TYR10
D	GLY11
D	THR12
D	ILE13
D	ALA54
D	ALA86
D	THR87
D	PRO88
D	GLY89
D	GLN109
D	GLY111
D	CYS141
D	ARG167
D	ASP170
D	GLN298
D	HOH610
D	HOH642
D	HOH675
D	HOH695
D	HOH696

Functional Information from PROSITE/UniProt

site_id	PS00071
Number of Residues	8
Details	GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. VSCNTTgL

Chain	Residue	Details
A	VAL139-LEU146

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Pyrococcus horikoshii ot3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1cf2

Chain	Residue	Details
A	CYS141
A	HIS217

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1cf2

Chain	Residue	Details
B	CYS141
B	HIS217

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1cf2

Chain	Residue	Details
C	CYS141
C	HIS217

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1cf2

Chain	Residue	Details
D	CYS141
D	HIS217

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)