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1H1Y

The structure of the cytosolic D-ribulose-5-phosphate 3-epimerase from rice complexed with sulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004750molecular_functionD-ribulose-phosphate 3-epimerase activity
A0005737cellular_componentcytoplasm
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
A0046872molecular_functionmetal ion binding
B0004750molecular_functionD-ribulose-phosphate 3-epimerase activity
B0005737cellular_componentcytoplasm
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
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A1224
ChainResidue
AGLY151
AGLY152
AGLY180
AGLY200
ASER201
AHOH2184
AHOH2213
AHOH2233
AHOH2234

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 B1224
ChainResidue
BGLY151
BGLY152
BGLY180
BGLY200
BSER201
BHOH2011
BHOH2176
BHOH2229
BHOH2230
BHOH2231
BHOH2233

Functional Information from PROSITE/UniProt
site_idPS01085
Number of Residues15
DetailsRIBUL_P_3_EPIMER_1 Ribulose-phosphate 3-epimerase family signature 1. LHMDImDghFVpNlT
ChainResidueDetails
ALEU35-THR49

site_idPS01086
Number of Residues23
DetailsRIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. VlVMTVePgfgGQkFmpemmeKV
ChainResidueDetails
AVAL141-VAL163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P32719
ChainResidueDetails
AASP38
BASP38

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P32719
ChainResidueDetails
AASP178
BASP178

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P32719
ChainResidueDetails
ASER11
AHIS69
AGLY149
AGLY200
BSER11
BHIS69
BGLY149
BGLY200

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12547196, ECO:0007744|PDB:1H1Z
ChainResidueDetails
AHIS36
AASP38
AASP178
BHIS36
BASP38
BASP178

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 270
ChainResidueDetails
ASER11electrostatic stabiliser, hydrogen bond donor, increase acidity
AHIS36metal ligand
AASP38hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
AMET40electrostatic stabiliser
AHIS69metal ligand
AMET71electrostatic stabiliser
AMET144electrostatic stabiliser
AASP178hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues8
DetailsM-CSA 270
ChainResidueDetails
BSER11electrostatic stabiliser, hydrogen bond donor, increase acidity
BHIS36metal ligand
BASP38hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
BMET40electrostatic stabiliser
BHIS69metal ligand
BMET71electrostatic stabiliser
BMET144electrostatic stabiliser
BASP178hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

220113

PDB entries from 2024-05-22

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