Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3OET

D-Erythronate-4-Phosphate Dehydrogenase complexed with NAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008615	biological_process	pyridoxine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0033711	molecular_function	4-phosphoerythronate dehydrogenase activity
A	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
A	0046983	molecular_function	protein dimerization activity
A	0051287	molecular_function	NAD binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008615	biological_process	pyridoxine biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0033711	molecular_function	4-phosphoerythronate dehydrogenase activity
B	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
B	0046983	molecular_function	protein dimerization activity
B	0051287	molecular_function	NAD binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008615	biological_process	pyridoxine biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0033711	molecular_function	4-phosphoerythronate dehydrogenase activity
C	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
C	0046983	molecular_function	protein dimerization activity
C	0051287	molecular_function	NAD binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008615	biological_process	pyridoxine biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0033711	molecular_function	4-phosphoerythronate dehydrogenase activity
D	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
D	0046983	molecular_function	protein dimerization activity
D	0051287	molecular_function	NAD binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0008615	biological_process	pyridoxine biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0033711	molecular_function	4-phosphoerythronate dehydrogenase activity
E	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
E	0046983	molecular_function	protein dimerization activity
E	0051287	molecular_function	NAD binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0008615	biological_process	pyridoxine biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0033711	molecular_function	4-phosphoerythronate dehydrogenase activity
F	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
F	0046983	molecular_function	protein dimerization activity
F	0051287	molecular_function	NAD binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0008615	biological_process	pyridoxine biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0033711	molecular_function	4-phosphoerythronate dehydrogenase activity
G	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
G	0046983	molecular_function	protein dimerization activity
G	0051287	molecular_function	NAD binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0008615	biological_process	pyridoxine biosynthetic process
H	0016491	molecular_function	oxidoreductase activity
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0033711	molecular_function	4-phosphoerythronate dehydrogenase activity
H	0036001	biological_process	'de novo' pyridoxal 5'-phosphate biosynthetic process
H	0046983	molecular_function	protein dimerization activity
H	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD A 379

Chain	Residue
A	ASN91
A	PRO148
A	HIS174
A	THR175
A	PRO176
A	TYR183
A	THR185
A	ALA206
A	CYS207
A	ARG208
A	ASP232
A	VAL95
A	HIS254
A	ALA256
A	GLY257
A	HOH382
A	HOH394
A	HOH401
A	HOH411
A	HOH422
A	GLY123
A	GLY125
A	ASN126
A	VAL127
A	CYS145
A	ASP146
A	PRO147

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD B 379

Chain	Residue
B	ASN91
B	VAL95
B	GLY123
B	GLY125
B	ASN126
B	VAL127
B	ASP146
B	PRO147
B	PRO148
B	HIS174
B	THR175
B	PRO176
B	TYR183
B	THR185
B	ALA206
B	CYS207
B	ARG208
B	ASP232
B	HIS254
B	ALA256
B	GLY257
B	HOH388
B	HOH403
B	HOH407
B	HOH555

site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD C 379

Chain	Residue
C	ASN91
C	VAL95
C	GLY123
C	VAL124
C	GLY125
C	ASN126
C	VAL127
C	ASP146
C	PRO147
C	PRO148
C	HIS174
C	THR175
C	PRO176
C	TYR178
C	TYR183
C	THR185
C	ALA206
C	CYS207
C	ARG208
C	ASP232
C	HIS254
C	ALA256
C	GLY257
C	HOH380
C	HOH393
C	HOH402
C	HOH423

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD D 379

Chain	Residue
D	HIS254
D	ALA256
D	GLY257
D	HOH398
D	HOH413
D	HOH414
D	HOH519
D	ASN91
D	VAL95
D	GLY123
D	GLY125
D	ASN126
D	VAL127
D	CYS145
D	ASP146
D	PRO147
D	PRO148
D	HIS174
D	THR175
D	PRO176
D	TYR178
D	TYR183
D	THR185
D	ALA206
D	CYS207
D	ARG208
D	ASP232

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD E 379

Chain	Residue
E	ASN91
E	VAL95
E	GLY123
E	GLY125
E	ASN126
E	VAL127
E	ASP146
E	PRO147
E	PRO148
E	ARG149
E	HIS174
E	THR175
E	PRO176
E	TYR178
E	TYR183
E	THR185
E	ALA206
E	CYS207
E	ARG208
E	ASP232
E	HIS254
E	ALA256
E	GLY257
E	HOH393
E	HOH440

site_id	AC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD F 379

Chain	Residue
F	ASN91
F	VAL95
F	GLY123
F	VAL124
F	GLY125
F	ASN126
F	VAL127
F	CYS145
F	ASP146
F	PRO147
F	PRO148
F	HIS174
F	THR175
F	PRO176
F	TYR178
F	TYR183
F	THR185
F	ALA206
F	CYS207
F	ASP232
F	HIS254
F	GLY257
F	HOH383
F	HOH404
F	HOH412

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD G 379

Chain	Residue
G	ASN91
G	VAL95
G	GLY123
G	VAL124
G	GLY125
G	ASN126
G	VAL127
G	CYS145
G	ASP146
G	PRO147
G	PRO148
G	HIS174
G	THR175
G	PRO176
G	TYR183
G	THR185
G	ALA206
G	CYS207
G	ARG208
G	ASP232
G	HIS254
G	ALA256
G	GLY257
G	HOH386
G	HOH393
G	HOH399

site_id	AC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD H 379

Chain	Residue
H	ASN91
H	VAL95
H	VAL122
H	GLY123
H	GLY125
H	ASN126
H	VAL127
H	CYS145
H	ASP146
H	PRO147
H	PRO148
H	HIS174
H	THR175
H	PRO176
H	TYR183
H	THR185
H	ALA206
H	CYS207
H	ARG208
H	ASP232
H	VAL233
H	HIS254
H	ALA256
H	GLY257
H	HOH383

Functional Information from PROSITE/UniProt

site_id	PS00065
Number of Residues	28
Details	D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGIVGvGNVGsrlqtrlealgir.TLlCD

Chain	Residue	Details
A	ILE119-ASP146

site_id	PS00671
Number of Residues	17
Details	D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LKpGaILINaCRGpVVD

Chain	Residue	Details
A	LEU197-ASP213

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01825","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01825","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01825","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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