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1PS8

Crystal Structure of the R270K Mutant of Aspartate Semialdehyde dehydrogenase from Haemophilus influenzae

Functional Information from GO Data
ChainGOidnamespacecontents
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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000269|PubMed:14559965, ECO:0000269|PubMed:15272161
ChainResidueDetails
ACYS136

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:14559965
ChainResidueDetails
AHIS277

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15272161
ChainResidueDetails
AARG10
ATHR37
AGLN74
ASER166
AGLN353

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14559965
ChainResidueDetails
AARG103
ALYS246

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:15272161
ChainResidueDetails
AGLN163
AGLU243
ALYS270

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1brm
ChainResidueDetails
ACYS136
AHIS277
AGLN163

226707

PDB entries from 2024-10-30

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