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1J5P

Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0009435biological_processNAD+ biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
A0019363biological_processpyridine nucleotide biosynthetic process
A0033735molecular_functionaspartate dehydrogenase [NAD(P)+] activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD A 300
ChainResidue
AGLY7
ASER57
APRO58
AALA60
AGLU63
ATYR64
AILE78
ASER79
AALA109
AASN164
AVAL165
AGLY9
ATHR223
AHOH313
AHOH314
AHOH367
AHOH375
AASN10
AILE11
AASP28
AARG29
AILE30
ACYS55
AALA56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000305|PubMed:12496312
ChainResidueDetails
AHIS193

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2, ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P
ChainResidueDetails
AASN10
AASP28
AALA56
AGLU63
AILE78

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2, ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P
ChainResidueDetails
AALA109
AASN164

237735

PDB entries from 2025-06-18

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