Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3Q0E

Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Vibrio Cholerae with product of S-allyl-L-cysteine sulfoxide

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 Residues7
DetailsBINDING SITE FOR RESIDUE CYS A 401
ChainResidue
AARG101
AASN133
ACYS134
AGLU240
ALYS243
AGLN350
AHOH809

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
ATHR36
ASER37
AHOH531
AHOH546
AARG9
ASER35

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 403
ChainResidue
AARG309
AHOH504
AHOH735
BLYS232

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
BARG9
BSER35
BTHR36
BSER37
BHOH548
BHOH787

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CYS B 402
ChainResidue
BARG101
BASN133
BCYS134
BGLU240
BGLN350
BHOH632
BHOH706

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
BARG19
BGLU22
BGLY323

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 404
ChainResidue
BGLY10
BMET11
BGLY167
BALA168
BHOH749
BHOH781

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon