Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3PZR

Crystals structure of aspartate beta-Semialdehyde dehydrogenase from Vibrio Cholerae with NADP and product of S-carbamoyl-L-cysteine

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 Residues10
DetailsBINDING SITE FOR RESIDUE CYS A 371
ChainResidue
AASN133
AHOH623
ACYS134
AGLN161
AGLY165
AILE229
AGLU240
AARG267
AHIS274
AGLN350

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CYS B 371
ChainResidue
BCYS134
BGLN161
BGLY165
BGLU240
BARG267
BHIS274
BGLN350
BNAP372
BHOH639

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAP A 372
ChainResidue
AGLY7
AARG9
AGLY10
AMET11
AVAL12
ASER35
ATHR36
ASER37
ACYS71
AGLN72
AHOH387
AHOH394
AHOH410
AHOH423
AHOH446
AHOH500
AHOH551
AHOH610

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 373
ChainResidue
AGLY210
APHE212
ATHR214
AHOH437
AHOH441
BHOH375

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAP B 372
ChainResidue
BGLY7
BARG9
BGLY10
BMET11
BVAL12
BTHR36
BSER37
BCYS71
BGLN72
BGLY73
BALA97
BGLY165
BGLN350
BCYS371
BHOH378
BHOH381
BHOH539
BHOH550
BHOH552
BHOH603
BHOH639
BHOH646
BHOH654
BHOH713

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 373
ChainResidue
BGLY210
BPHE212
BHOH438
BHOH445
BHOH454
BHOH458

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
DetailsActive site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"12493825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12493825","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12493825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12493825","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"S-cysteinyl cysteine; in inhibited form"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon