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2GZ3

Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with NADP and aspartate-semialdehyde

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
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
B0000166molecular_functionnucleotide binding
B0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
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
C0000166molecular_functionnucleotide binding
C0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
C0008652biological_processamino acid biosynthetic process
C0009085biological_processlysine biosynthetic process
C0009086biological_processmethionine biosynthetic process
C0009088biological_processthreonine biosynthetic process
C0009089biological_processlysine biosynthetic process via diaminopimelate
C0009097biological_processisoleucine biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0019877biological_processdiaminopimelate biosynthetic process
C0046983molecular_functionprotein dimerization activity
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
C0071266biological_process'de novo' L-methionine biosynthetic process
D0000166molecular_functionnucleotide binding
D0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
D0008652biological_processamino acid biosynthetic process
D0009085biological_processlysine biosynthetic process
D0009086biological_processmethionine biosynthetic process
D0009088biological_processthreonine biosynthetic process
D0009089biological_processlysine biosynthetic process via diaminopimelate
D0009097biological_processisoleucine biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0019877biological_processdiaminopimelate biosynthetic process
D0046983molecular_functionprotein dimerization activity
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
D0071266biological_process'de novo' L-methionine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAP A 367
ChainResidue
AGLY9
ATHR57
ASER71
AALA72
AGLY73
ATHR76
AASN94
ATHR95
ASER158
AGLY159
AGLY161
ATHR11
AMET162
AASN325
ALEU326
AGLY329
AALA330
AAS2400
AHOH479
AHOH504
AHOH557
AGLY12
AALA13
AVAL14
AALA36
ASER37
AARG39
ASER40

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AS2 A 400
ChainResidue
AASN127
ACYS128
AGLN155
AGLY159
AILE209
AGLU220
AARG245
AHIS252
ANAP367
AHOH608

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAP B 367
ChainResidue
BGLY9
BTHR11
BGLY12
BALA13
BVAL14
BALA36
BSER37
BSER40
BTHR57
BSER71
BALA72
BGLY73
BTHR76
BASN94
BSER158
BGLY159
BGLY161
BMET162
BASN325
BLEU326
BAS2400
BHOH442
BHOH467
BHOH512
DLYS86

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AS2 B 400
ChainResidue
BASN127
BCYS128
BGLN155
BGLY159
BILE209
BGLU220
BARG245
BHIS252
BNAP367

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAP C 367
ChainResidue
ALYS86
CGLY9
CTHR11
CGLY12
CALA13
CVAL14
CALA36
CSER37
CARG39
CSER40
CTHR57
CSER71
CALA72
CGLY73
CTHR76
CASN94
CTHR95
CSER158
CGLY159
CGLY161
CMET162
CLEU326
CAS2400
CHOH500

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AS2 C 400
ChainResidue
CGLY159
CILE209
CGLU220
CARG245
CHIS252
CNAP367
CASN127
CCYS128
CGLN155

site_idAC7
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAP D 367
ChainResidue
DGLY9
DTHR11
DGLY12
DALA13
DVAL14
DALA36
DSER37
DARG39
DSER40
DTHR57
DSER71
DALA72
DGLY73
DSER74
DTHR76
DASN94
DTHR95
DSER158
DGLY159
DGLY161
DMET162
DASN325
DLEU326
DGLY329
DALA330
DAS2400
DHOH539
DHOH540

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AS2 D 400
ChainResidue
DASN127
DCYS128
DGLN155
DGLY159
DILE209
DGLU220
DARG245
DHIS252
DNAP367

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
AGLN155
AHIS252
ACYS128

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
BGLN155
BHIS252
BCYS128

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
CGLN155
CHIS252
CCYS128

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
DGLN155
DHIS252
DCYS128

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
AGLN155
ACYS128

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
BGLN155
BCYS128

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
CGLN155
CCYS128

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
DGLN155
DCYS128

222036

PDB entries from 2024-07-03

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