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4XB1

Hyperthermophilic archaeal homoserine dehydrogenase in complex with NADPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004412molecular_functionhomoserine dehydrogenase activity
A0006520biological_processamino acid metabolic process
A0008652biological_processamino acid biosynthetic process
A0009086biological_processmethionine biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
A0070403molecular_functionNAD+ binding
B0000166molecular_functionnucleotide binding
B0004412molecular_functionhomoserine dehydrogenase activity
B0006520biological_processamino acid metabolic process
B0008652biological_processamino acid biosynthetic process
B0009086biological_processmethionine biosynthetic process
B0009088biological_processthreonine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
B0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue NDP A 1001
ChainResidue
APHE8
ASER92
ASER93
ASER114
AASN115
ALYS116
ASER141
AGLY295
AGLY296
ATHR300
AMPD1003
APHE10
AHOH1143
AHOH1161
AHOH1170
AHOH1201
AHOH1205
AHOH1211
AHOH1213
AHOH1219
AGLY11
ATHR12
AVAL13
AASP39
AARG40
ALYS57
AVAL91

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 1002
ChainResidue
AGLU140
AVAL143
AMET144
AALA145
ATHR147

site_idAC3
Number of Residues7
Detailsbinding site for residue MPD A 1003
ChainResidue
ALYS116
ALYS215
AGLY294
ANDP1001
AHOH1144
AHOH1188
AHOH1201

site_idAC4
Number of Residues3
Detailsbinding site for residue MPD A 1004
ChainResidue
ALYS131
AGLY225
ALEU318

site_idAC5
Number of Residues23
Detailsbinding site for residue NDP B 1001
ChainResidue
BPHE8
BPHE10
BGLY11
BTHR12
BVAL13
BASP39
BARG40
BLYS57
BVAL91
BSER92
BSER93
BSER114
BASN115
BLYS116
BSER141
BGLY295
BGLY296
BTHR300
BMPD1003
BHOH1125
BHOH1163
BHOH1174
BHOH1188

site_idAC6
Number of Residues5
Detailsbinding site for residue NA B 1002
ChainResidue
BGLU140
BVAL143
BMET144
BALA145
BTHR147

site_idAC7
Number of Residues6
Detailsbinding site for residue MPD B 1003
ChainResidue
BLYS116
BLYS215
BGLY294
BNDP1001
BHOH1163
BHOH1178

site_idAC8
Number of Residues5
Detailsbinding site for residue MPD B 1004
ChainResidue
AASN73
AGLU78
BASN267
BHOH1103
BHOH1109

site_idAC9
Number of Residues2
Detailsbinding site for residue MPD B 1005
ChainResidue
BMET127
BGLY225

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PIRSR","id":"PIRSR036497-1","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26154028","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4XB1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XB2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26154028","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4XB1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"F9VNG5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P31116","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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