Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CF2

THREE-DIMENSIONAL STRUCTURE OF D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON METHANOTHERMUS FERVIDUS

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 P 1001

Chain	Residue
P	SER139
P	CYS140
P	ASN141
P	ARG167
P	HIS193
P	HIS194
P	HOH1216

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 R 1002

Chain	Residue
R	ASN141
R	ARG167
R	HIS193
R	HIS194
R	SER139
R	CYS140

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 O 1003

Chain	Residue
O	SER139
O	CYS140
O	ASN141
O	ARG167
O	HIS193
O	HIS194
O	HOH1045
O	HOH1126

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 Q 1004

Chain	Residue
Q	SER139
Q	CYS140
Q	ASN141
Q	ARG167
Q	HIS193
Q	HIS194
Q	HOH1212

site_id	AC5
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAP P 340

Chain	Residue
P	ASN7
P	GLY8
P	TYR9
P	GLY10
P	THR11
P	VAL12
P	LYS33
P	THR34
P	ARG35
P	ALA53
P	CYS85
P	THR86
P	PRO87
P	GLU88
P	ILE90
P	GLN108
P	GLY110
P	ARG168
P	ASP171
P	GLN300
P	HOH1048
P	HOH1053
P	HOH1061
P	HOH1069
P	HOH1078
P	HOH1088
P	HOH1096
P	HOH1097
P	HOH1104
P	HOH1107
P	HOH1109
P	HOH1111
P	HOH1165
P	HOH1229
P	HOH1232

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP R 340

Chain	Residue
R	ASN7
R	GLY8
R	TYR9
R	GLY10
R	THR11
R	VAL12
R	LYS33
R	THR34
R	ARG35
R	CYS85
R	THR86
R	PRO87
R	GLU88
R	GLN108
R	GLY110
R	ASP171
R	GLN300
R	HOH1006
R	HOH1008
R	HOH1012
R	HOH1015
R	HOH1016
R	HOH1018
R	HOH1104
R	HOH1112
R	HOH1176

site_id	AC7
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAP O 340

Chain	Residue
O	THR86
O	PRO87
O	GLU88
O	GLN108
O	GLY110
O	ASP171
O	GLN300
O	ILE304
O	HOH1029
O	HOH1039
O	HOH1048
O	HOH1061
O	HOH1066
O	HOH1071
O	HOH1078
O	HOH1085
O	HOH1103
O	HOH1106
O	HOH1161
O	HOH1172
O	HOH1192
O	ASN7
O	GLY8
O	TYR9
O	GLY10
O	THR11
O	VAL12
O	LYS33
O	THR34
O	ARG35
O	CYS85

site_id	AC8
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAP Q 340

Chain	Residue
Q	ASN7
Q	GLY8
Q	TYR9
Q	GLY10
Q	THR11
Q	VAL12
Q	LYS33
Q	THR34
Q	ARG35
Q	CYS85
Q	THR86
Q	PRO87
Q	GLU88
Q	ILE90
Q	GLN108
Q	GLY110
Q	ARG168
Q	ASP171
Q	GLN300
Q	ILE304
Q	HOH1051
Q	HOH1064
Q	HOH1079
Q	HOH1087
Q	HOH1088
Q	HOH1099
Q	HOH1104
Q	HOH1109
Q	HOH1112
Q	HOH1124
Q	HOH1202
Q	HOH1213

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
P	VAL138-LEU145

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":"PubMed","id":"10715215","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10715215

Chain	Residue	Details
O	CYS140
O	HIS219

site_id	CSA2
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10715215

Chain	Residue	Details
P	CYS140
P	HIS219

site_id	CSA3
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10715215

Chain	Residue	Details
R	CYS140
R	HIS219

site_id	CSA4
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10715215

Chain	Residue	Details
Q	CYS140
Q	HIS219

site_id	MCSA1
Number of Residues	2
Details	M-CSA 619

Chain

Residue

Details

site_id	MCSA2
Number of Residues	2
Details	M-CSA 619

Chain

Residue

Details

site_id	MCSA3
Number of Residues	2
Details	M-CSA 619

Chain

Residue

Details

site_id	MCSA4
Number of Residues	2
Details	M-CSA 619

Chain

Residue

Details

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