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1Q2X

Crystal Structure of the E243D Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae bound with substrate aspartate semialdehyde

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 PROSITE/UniProt
site_idPS01103
Number of Residues15
DetailsASD Aspartate-semialdehyde dehydrogenase signature. VDglCvRIgalrCHS
ChainResidueDetails
AVAL264-SER278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000269|PubMed:14559965, ECO:0000269|PubMed:15272161
ChainResidueDetails
AHTI136
BHTI136

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:14559965
ChainResidueDetails
AHIS277
BHIS277

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15272161
ChainResidueDetails
AARG10
BGLN353
ATHR37
AGLN74
ASER166
AGLN353
BARG10
BTHR37
BGLN74
BSER166

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14559965
ChainResidueDetails
AARG103
ALYS246
BARG103
BLYS246

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:15272161
ChainResidueDetails
AGLN163
AASP243
AARG270
BGLN163
BASP243
BARG270

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
AHIS277
AGLN163

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
BHIS277
BGLN163

224004

PDB entries from 2024-08-21

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