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5KXJ

Crystal Structure of L-Aspartate Oxidase from Salmonella typhimurium in the Complex with Substrate L-Aspartate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0008734molecular_functionL-aspartate oxidase activity
A0009435biological_processNAD biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0034628biological_process'de novo' NAD biosynthetic process from aspartate
A0044318molecular_functionL-aspartate:fumarate oxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GOL A 601
ChainResidue
AGLY76
AILE77
ACYS78
AHOH839

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 602
ChainResidue
AASN150
AILE63
AGLU84
ASER88
ASER146
AGLN149

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 603
ChainResidue
AGLN212
ATYR213
ATHR214
AASN255
AARG444

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 604
ChainResidue
AARG26
ATHR92
ATRP96
ATRP400
AEDO606
AHOH747
AHOH784

site_idAC5
Number of Residues9
Detailsbinding site for residue EDO A 605
ChainResidue
AHIS81
APHE85
AGLN149
AASN150
AHIS151
APRO152
AASP361
AHOH728
AHOH778

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 606
ChainResidue
AGLU29
ATRP96
AGLN100
AEDO604
AHOH774

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 607
ChainResidue
AASP164
AARG230
AARG491
AHOH879
AHOH887

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 A 608
ChainResidue
ALYS198
AVAL413
AHIS414
ASER415

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 609
ChainResidue
AARG234
AGLU424
AILE530
AHOH756

site_idAD1
Number of Residues14
Detailsbinding site for residue ASP A 610
ChainResidue
AGLY17
AALA18
AALA19
AGLY374
AGLU375
ASER391
ALEU392
ACYS395
AHOH704
AHOH710
AHOH712
AHOH739
AHOH752
AHOH844

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P10902
ChainResidueDetails
AARG290

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P10902
ChainResidueDetails
ALYS38
ASER45
AASP223
AGLU375
ASER391
ASER16

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important in orienting the L-aspartate substrate => ECO:0000250|UniProtKB:P10902
ChainResidueDetails
AGLU121

219869

PDB entries from 2024-05-15

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