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1TA4

Crystal Structure Of Aspartate-Semialdehyde Dehydrogenase From Haemophilus Influenzae with a Bound Arsenate

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ART A 373
ChainResidue
AARG102
AASN134
ACYS135
ALYS244
AART374
AHOH431

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ART A 374
ChainResidue
ALYS244
AART373
ASER99
AASP231
ALYS240

Functional Information from PROSITE/UniProt
site_idPS01103
Number of Residues15
DetailsASD Aspartate-semialdehyde dehydrogenase signature. VDglCvRIgalrCHS
ChainResidueDetails
AVAL261-SER275

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
ACYS135

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:14559965
ChainResidueDetails
AHIS274

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15272161
ChainResidueDetails
ATHR37
AGLN73
ASER165
AGLN350
AARG10

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14559965
ChainResidueDetails
AARG102
ALYS244

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:15272161
ChainResidueDetails
AARG267
AGLN162
AGLU241

219869

PDB entries from 2024-05-15

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