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Crystal structure of aspartate semialdehyde dehydrogenase from vibrio cholerae with NADP and S-methyl-l-cysteine sulfoxide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
A0006520biological_processamino acid metabolic process
A0008652biological_processamino acid biosynthetic process
A0009067biological_processaspartate family amino 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
B0009067biological_processaspartate family amino 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 Residues9
DetailsBINDING SITE FOR RESIDUE CYS A 500
ChainResidue
AASN133
ACYS134
AGLN161
AGLY165
AGLU240
AARG267
AHIS274
AGLN350
ANDP502

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CYS B 501
ChainResidue
BASN133
BCYS134
BGLN161
BGLY165
BGLU240
BARG267
BHIS274
BGLN350
BNDP503

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NDP A 502
ChainResidue
AGLY7
AARG9
AGLY10
AMET11
AVAL12
ATHR36
ASER37
ACYS71
AGLN72
AGLY73
AALA97
ASER164
AGLY165
AGLN350
ALEU351
AGLY354
ACYS500
AHOH510
AHOH523
AHOH526
AHOH527
AHOH562
AHOH643
AHOH665
AHOH687

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NDP B 503
ChainResidue
APRO192
BGLY7
BARG9
BGLY10
BMET11
BVAL12
BSER35
BTHR36
BSER37
BCYS71
BGLN72
BGLY73
BALA97
BSER164
BGLY165
BGLN350
BLEU351
BGLY354
BCYS501
BHOH537
BHOH538
BHOH553
BHOH663
BHOH674
BHOH679

Functional Information from PROSITE/UniProt
site_idPS01103
Number of Residues15
DetailsASD Aspartate-semialdehyde dehydrogenase signature. IDgtCvRIgamrCHS
ChainResidueDetails
AILE261-SER275

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000269|PubMed:12493825
ChainResidueDetails
ACYS134
BCYS134

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:12493825
ChainResidueDetails
AHIS274
BHIS274

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12493825
ChainResidueDetails
AARG9
BSER164
BPRO192
BGLN350
ATHR36
AGLN72
ASER164
APRO192
AGLN350
BARG9
BTHR36
BGLN72

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02121
ChainResidueDetails
AARG101
ALYS243
BARG101
BLYS243

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:12493825
ChainResidueDetails
AGLN161
AGLU240
AARG267
BGLN161
BGLU240
BARG267

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-cysteinyl cysteine; in inhibited form
ChainResidueDetails
ACYS134
BCYS134

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
AHIS274
ACYS134
AGLN161

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
BHIS274
BCYS134
BGLN161

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PDB entries from 2025-07-02

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