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3OVP

Crystal Structure of hRPE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004750molecular_functionD-ribulose-phosphate 3-epimerase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006098biological_processpentose-phosphate shunt
A0009052biological_processpentose-phosphate shunt, non-oxidative branch
A0016853molecular_functionisomerase activity
A0016857molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
B0004750molecular_functionD-ribulose-phosphate 3-epimerase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006098biological_processpentose-phosphate shunt
B0009052biological_processpentose-phosphate shunt, non-oxidative branch
B0016853molecular_functionisomerase activity
B0016857molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 A 229
ChainResidue
AHIS35
AASP37
AHIS70
AASP175
AHOH258
AHOH266

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE XPE A 230
ChainResidue
AASP171
AMET193
AGLY4
ALYS6
AASP32

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE XPE A 231
ChainResidue
APRO121
AMET153
AHOH325

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE XPE A 232
ChainResidue
AHIS184
ALYS185
AHOH238

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 B 229
ChainResidue
BHIS35
BASP37
BHIS70
BASP175
BHOH256
BHOH261

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE XPE B 230
ChainResidue
BGLY4
BLYS6
BASP32
BPHE66
BASP171

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE XPE B 231
ChainResidue
BGLN63
BGLY87
BALA88
BGLY112

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE XPE B 232
ChainResidue
BGLU126
BTRP162

Functional Information from PROSITE/UniProt
site_idPS01085
Number of Residues15
DetailsRIBUL_P_3_EPIMER_1 Ribulose-phosphate 3-epimerase family signature 1. LHLDVmDghFVpNiT
ChainResidueDetails
ALEU34-THR48

site_idPS01086
Number of Residues23
DetailsRIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. AlVMTVePgfgGQkFmedmmpKV
ChainResidueDetails
AALA138-VAL160

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:20923965, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR
ChainResidueDetails
AASP37
BASP37

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:20923965, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR
ChainResidueDetails
AASP175
BASP175

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20923965, ECO:0007744|PDB:3OVR
ChainResidueDetails
ASER10
BSER10

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20923965, ECO:0000269|Ref.9, ECO:0007744|PDB:3OVP, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR, ECO:0007744|PDB:3QC3
ChainResidueDetails
AHIS35
AASP37
AASP175
BHIS35
BASP37
BASP175

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20923965, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR
ChainResidueDetails
AHIS70
AGLY146
AGLY197
BHIS70
BGLY146
BGLY197

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2

226707

PDB entries from 2024-10-30

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