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1USL

Structure Of Mycobacterium tuberculosis Ribose-5-Phosphate Isomerase, RpiB, Rv2465c, Complexed With Phosphate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004751molecular_functionribose-5-phosphate isomerase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006098biological_processpentose-phosphate shunt
A0009052biological_processpentose-phosphate shunt, non-oxidative branch
A0016853molecular_functionisomerase activity
A0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
A0019316biological_processD-allose catabolic process
B0004751molecular_functionribose-5-phosphate isomerase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006098biological_processpentose-phosphate shunt
B0009052biological_processpentose-phosphate shunt, non-oxidative branch
B0016853molecular_functionisomerase activity
B0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
B0019316biological_processD-allose catabolic process
C0004751molecular_functionribose-5-phosphate isomerase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005975biological_processcarbohydrate metabolic process
C0006098biological_processpentose-phosphate shunt
C0009052biological_processpentose-phosphate shunt, non-oxidative branch
C0016853molecular_functionisomerase activity
C0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
C0019316biological_processD-allose catabolic process
D0004751molecular_functionribose-5-phosphate isomerase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005975biological_processcarbohydrate metabolic process
D0006098biological_processpentose-phosphate shunt
D0009052biological_processpentose-phosphate shunt, non-oxidative branch
D0016853molecular_functionisomerase activity
D0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
D0019316biological_processD-allose catabolic process
E0004751molecular_functionribose-5-phosphate isomerase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005975biological_processcarbohydrate metabolic process
E0006098biological_processpentose-phosphate shunt
E0009052biological_processpentose-phosphate shunt, non-oxidative branch
E0016853molecular_functionisomerase activity
E0016861molecular_functionintramolecular oxidoreductase activity, interconverting aldoses and ketoses
E0019316biological_processD-allose catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A1159
ChainResidue
AARG137
AARG141
AHOH2110
AHOH2111
AHOH2112
BHIS12
BARG113

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B1159
ChainResidue
AHOH2007
BARG137
BHIS138
BARG141
BHOH2114
BHOH2115
BHOH2116
AHIS12
AALA13

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 C1161
ChainResidue
CARG137
CARG141
CHOH2110
CHOH2111
DHIS12
DHOH2005

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 D1159
ChainResidue
CHIS12
CHOH2004
DARG137
DHIS138
DARG141
DHOH2137
DHOH2138
DHOH2139

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 E1159
ChainResidue
EHIS12
EARG137
EHIS138
EARG141
EHOH2100
EHOH2101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:15590681, ECO:0000305|PubMed:18640127, ECO:0007744|PDB:2BES, ECO:0007744|PDB:2BET, ECO:0007744|PDB:2VVO, ECO:0007744|PDB:2VVP, ECO:0007744|PDB:2VVQ
ChainResidueDetails
AGLU75
BGLU75
CGLU75
DGLU75
EGLU75

site_idSWS_FT_FI2
Number of Residues5
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:15590681, ECO:0000305|PubMed:18640127, ECO:0007744|PDB:2BES, ECO:0007744|PDB:2BET, ECO:0007744|PDB:2VVO, ECO:0007744|PDB:2VVP, ECO:0007744|PDB:2VVQ
ChainResidueDetails
AHIS102
BHIS102
CHIS102
DHIS102
EHIS102

site_idSWS_FT_FI3
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:14687575, ECO:0000269|PubMed:15590681, ECO:0000269|PubMed:18640127, ECO:0007744|PDB:1USL, ECO:0007744|PDB:2BES, ECO:0007744|PDB:2BET, ECO:0007744|PDB:2VVO, ECO:0007744|PDB:2VVP, ECO:0007744|PDB:2VVQ
ChainResidueDetails
AASP11
DASP11
DARG113
DARG137
EASP11
EARG113
EARG137
AARG113
AARG137
BASP11
BARG113
BARG137
CASP11
CARG113
CARG137

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15590681, ECO:0000269|PubMed:18640127, ECO:0007744|PDB:2BES, ECO:0007744|PDB:2BET, ECO:0007744|PDB:2VVO, ECO:0007744|PDB:2VVP, ECO:0007744|PDB:2VVQ
ChainResidueDetails
AGLY70
BGLY70
CGLY70
DGLY70
EGLY70

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15590681, ECO:0000269|PubMed:18640127, ECO:0007744|PDB:2BET, ECO:0007744|PDB:2VVO, ECO:0007744|PDB:2VVP
ChainResidueDetails
AASN103
BASN103
CASN103
DASN103
EASN103

site_idSWS_FT_FI6
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:14687575, ECO:0000269|PubMed:18640127, ECO:0007744|PDB:1USL, ECO:0007744|PDB:2VVO, ECO:0007744|PDB:2VVP, ECO:0007744|PDB:2VVQ
ChainResidueDetails
AARG141
BARG141
CARG141
DARG141
EARG141

218853

PDB entries from 2024-04-24

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