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4R5M

Crystal structure of Vc-Aspartate beta-semialdehyde-dehydrogenase with NADP and 4-Nitro-2-Phosphono-Benzoic acid

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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A 401
ChainResidue
AGLY210
APHE212
ATHR214
AHOH533
AHOH640
AHOH698

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAP A 402
ChainResidue
AMET11
AVAL12
ATHR36
ASER37
ACYS71
AGLN72
AGLY73
ASER164
AGLY165
AGLN350
A4NO403
AHOH504
AHOH569
AHOH571
AHOH625
AHOH646
AHOH651
AHOH687
AHOH777
AHOH806
AHOH844
AGLY7
AARG9
AGLY10

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 4NO A 403
ChainResidue
ACYS71
AGLY73
AGLY74
AALA96
AALA97
ASER98
AARG101
AASN133
ALYS243
ANAP402
AHOH747

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NAP B 401
ChainResidue
APRO192
AHOH796
BGLY7
BARG9
BGLY10
BMET11
BVAL12
BTHR36
BSER37
BCYS71
BGLN72
BGLY165
B4NO402
BHOH584
BHOH586
BHOH622
BHOH669

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 4NO B 402
ChainResidue
BGLY74
BALA96
BALA97
BSER98
BARG101
BASN133
BNAP401

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
AGLN72
ASER164
APRO192
AGLN350
BARG9
BTHR36
BGLN72
BSER164
BPRO192
BGLN350
AARG9
ATHR36

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

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

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

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PDB entries from 2024-06-12

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