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2E5V

Crystal structure of L-Aspartate Oxidase from hyperthermophilic archaeon Sulfolobus tokodaii

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
B0000166molecular_functionnucleotide binding
B0005737cellular_componentcytoplasm
B0008734molecular_functionL-aspartate oxidase activity
B0009435biological_processNAD biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0019363biological_processpyridine nucleotide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 2001
ChainResidue
AARG348
ASER351
AFAD1002
AHOH2175

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 2002
ChainResidue
BARG348
BSER351
BFAD1001
BHOH2154

site_idAC3
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 1002
ChainResidue
AGLY6
ASER7
AGLY8
AILE9
AALA10
ASER29
ALYS30
AARG31
AGLY35
ASER36
ATHR37
AALA40
AGLY42
AGLY43
AASP139
ALEU141
AALA171
ATHR172
ASER183
AASN188
AASP191
AHIS313
APHE314
AGLY336
AGLU337
AARG348
ASER351
ASER353
ALEU354
ACL2001
AHOH2014
AHOH2024
AHOH2031
AHOH2038
AHOH2078
AILE5

site_idAC4
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD B 1001
ChainResidue
BILE5
BGLY6
BSER7
BGLY8
BILE9
BALA10
BSER29
BLYS30
BARG31
BGLY35
BSER36
BTHR37
BALA40
BGLY42
BGLY43
BLEU141
BALA171
BTHR172
BGLY173
BSER183
BASN188
BASP191
BHIS313
BPHE314
BGLY336
BGLU337
BARG348
BSER351
BSER353
BLEU354
BCL2002
BHOH2007
BHOH2021
BHOH2031
BHOH2032
BHOH2047

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P10902
ChainResidueDetails
AARG257
BARG257

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:18226609, ECO:0007744|PDB:2E5V
ChainResidueDetails
ASER7
BSER36
BGLY42
BASP191
BGLU337
BSER353
ASER29
ASER36
AGLY42
AASP191
AGLU337
ASER353
BSER7
BSER29

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important in orienting the L-aspartate substrate => ECO:0000250|UniProtKB:P10902
ChainResidueDetails
AGLU102
BGLU102

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
AHIS212
AARG348
AHIS313
AARG257

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
BHIS212
BARG348
BHIS313
BARG257

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PDB entries from 2024-11-13

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