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4X84

Crystal structure of Ribose-5-phosphate isomerase A from Pseudomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0004751molecular_functionribose-5-phosphate isomerase activity
A0005829cellular_componentcytosol
A0006014biological_processD-ribose metabolic process
A0006098biological_processpentose-phosphate shunt
A0009052biological_processpentose-phosphate shunt, non-oxidative branch
A0016853molecular_functionisomerase activity
A0044281biological_processsmall molecule metabolic process
B0004751molecular_functionribose-5-phosphate isomerase activity
B0005829cellular_componentcytosol
B0006014biological_processD-ribose metabolic process
B0006098biological_processpentose-phosphate shunt
B0009052biological_processpentose-phosphate shunt, non-oxidative branch
B0016853molecular_functionisomerase activity
B0044281biological_processsmall molecule metabolic process
C0004751molecular_functionribose-5-phosphate isomerase activity
C0005829cellular_componentcytosol
C0006014biological_processD-ribose metabolic process
C0006098biological_processpentose-phosphate shunt
C0009052biological_processpentose-phosphate shunt, non-oxidative branch
C0016853molecular_functionisomerase activity
C0044281biological_processsmall molecule metabolic process
D0004751molecular_functionribose-5-phosphate isomerase activity
D0005829cellular_componentcytosol
D0006014biological_processD-ribose metabolic process
D0006098biological_processpentose-phosphate shunt
D0009052biological_processpentose-phosphate shunt, non-oxidative branch
D0016853molecular_functionisomerase activity
D0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue FLC A 300
ChainResidue
ATHR32
ALYS125
AHOH502
AHOH507
AHOH514
AHOH521
AHOH579
AHOH585
AHOH705
ASER34
ATHR35
AALA87
AASP88
ALYS98
AGLY99
AGLY100
AGLY101

site_idAC2
Number of Residues16
Detailsbinding site for residue FLC B 300
ChainResidue
BTHR32
BSER34
BTHR35
BALA87
BASP88
BLYS98
BGLY99
BGLY100
BGLY101
BLYS125
BHOH491
BHOH497
BHOH517
BHOH572
BHOH685
BHOH711

site_idAC3
Number of Residues15
Detailsbinding site for residue FLC C 300
ChainResidue
CTHR32
CSER34
CTHR35
CALA87
CASP88
CLYS98
CGLY99
CGLY100
CGLY101
CHOH481
CHOH533
CHOH622
CHOH661
CHOH748
CHOH749

site_idAC4
Number of Residues16
Detailsbinding site for residue FLC D 300
ChainResidue
DTHR32
DSER34
DTHR35
DALA87
DASP88
DLYS98
DGLY99
DGLY100
DGLY101
DLYS125
DHOH489
DHOH508
DHOH514
DHOH526
DHOH561
DHOH586

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00170
ChainResidueDetails
AGLU107
BGLU107
CGLU107
DGLU107

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00170
ChainResidueDetails
ATHR32
CASP85
CLYS98
CLYS125
DTHR32
DASP85
DLYS98
DLYS125
AASP85
ALYS98
ALYS125
BTHR32
BASP85
BLYS98
BLYS125
CTHR32

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PDB entries from 2025-06-18

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