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1YS4

Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii

Functional Information from GO Data
ChainGOidnamespacecontents
A0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
A0006520biological_processamino acid metabolic process
A0008652biological_processamino acid biosynthetic process
A0009085biological_processlysine biosynthetic process
A0009086biological_processmethionine biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009097biological_processisoleucine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0019877biological_processdiaminopimelate biosynthetic process
A0046983molecular_functionprotein dimerization activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0071266biological_process'de novo' L-methionine biosynthetic process
B0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
B0006520biological_processamino acid metabolic process
B0008652biological_processamino acid biosynthetic process
B0009085biological_processlysine biosynthetic process
B0009086biological_processmethionine biosynthetic process
B0009088biological_processthreonine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009097biological_processisoleucine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0019877biological_processdiaminopimelate biosynthetic process
B0046983molecular_functionprotein dimerization activity
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B0071266biological_process'de novo' L-methionine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAP A 900
ChainResidue
AGLY15
APRO92
ALEU95
AASN113
ASER187
AGLY188
AALA189
AGLY190
AASN333
ATHR334
AALA338
ATHR17
AMLA904
AHOH934
AHOH983
AHOH986
AHOH995
AHOH1025
AHOH1038
AHOH1068
AGLY18
ASER19
AVAL20
AALA41
ASER42
ASER45
ATHR74

site_idAC2
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAP B 901
ChainResidue
BGLY15
BTHR17
BGLY18
BSER19
BVAL20
BALA41
BSER42
BSER45
BTHR74
BALA90
BLEU91
BPRO92
BLEU95
BASN113
BGLY188
BGLY190
BASN333
BTHR334
BALA338
BMLA902
BHOH944
BHOH986
BHOH990
BHOH1011
BHOH1020
BHOH1051
BHOH1055
BHOH1092
BHOH1094
BHOH1121

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MLA B 902
ChainResidue
BASN113
BARG118
BASN156
BCYS157
BLYS213
BNAP901
BHOH951
BHOH1020

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLA A 903
ChainResidue
APHE206
AILE207
AASN209
AGLU210
AGLU211
AGLU212
AHOH914
AHOH964
AHOH1096
BARG316

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLA A 904
ChainResidue
ASER115
AARG118
AASN156
ACYS157
ALYS213
ANAP900
AHOH922
AHOH940
AHOH1025

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MLA B 905
ChainResidue
AARG316
BPHE206
BILE207
BASN209
BGLU210
BGLU211
BGLU212
BHOH918
BHOH989
BHOH1053
BHOH1060
BHOH1066

Functional Information from PROSITE/UniProt
site_idPS01103
Number of Residues15
DetailsASD Aspartate-semialdehyde dehydrogenase signature. ISasCnRVavidGHT
ChainResidueDetails
AILE237-THR251

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000305|PubMed:16225889
ChainResidueDetails
ACYS157
BCYS157

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:16225889
ChainResidueDetails
AHIS250
BHIS250

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16225889
ChainResidueDetails
ATHR17
ASER42
ASER187
AASN333
BTHR17
BSER42
BSER187
BASN333

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02121
ChainResidueDetails
AARG118
BARG243
AGLN184
AGLU210
ALYS213
AARG243
BARG118
BGLN184
BGLU210
BLYS213

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
AGLN184
ACYS157
AHIS250

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
BGLN184
BCYS157
BHIS250

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
AGLN184
ACYS157

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
BGLN184
BCYS157

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PDB entries from 2024-10-16

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