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3VNK

Crystal structures of D-Psicose 3-epimerase with D-fructose from Clostridium cellulolyticum H10

Functional Information from GO Data
ChainGOidnamespacecontents
A0016853molecular_functionisomerase activity
A0016857molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
B0016853molecular_functionisomerase activity
B0016857molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
C0016853molecular_functionisomerase activity
C0016857molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives
C0030145molecular_functionmanganese ion binding
C0046872molecular_functionmetal ion binding
C0050897molecular_functioncobalt ion binding
D0016853molecular_functionisomerase activity
D0016857molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives
D0030145molecular_functionmanganese ion binding
D0046872molecular_functionmetal ion binding
D0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FUD A 301
ChainResidue
ATYR6
APHE246
AMN302
AHOH401
AHOH591
ATRP112
AGLU150
AGLU156
AASP183
AHIS186
AHIS209
AARG215
AGLU244

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 302
ChainResidue
AGLU150
AASP183
AHIS209
AGLU244
AFUD301

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FUD B 1301
ChainResidue
BTYR6
BTRP14
BTRP112
BGLU150
BGLU156
BASP183
BHIS186
BHIS209
BARG215
BGLU244
BMN1302
BHOH1450
BHOH1491
BHOH1591

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 1302
ChainResidue
BGLU150
BASP183
BHIS209
BGLU244
BFUD1301

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 1303
ChainResidue
BASP192
BHOH1583
CHOH450
DHOH500

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FUD C 301
ChainResidue
CTYR6
CTRP14
CTRP112
CGLU150
CGLU156
CASP183
CHIS186
CHIS209
CARG215
CGLU244
CMN302
CHOH422
CHOH424
CHOH547

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 302
ChainResidue
CGLU150
CASP183
CHIS209
CGLU244
CFUD301

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN C 303
ChainResidue
BHOH1583
CARG220

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FUD D 301
ChainResidue
DTYR6
DTRP14
DTRP112
DGLU150
DGLU156
DASP183
DHIS186
DHIS209
DARG215
DGLU244
DMN302
DHOH405
DHOH437
DHOH453

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN D 302
ChainResidue
DGLU150
DASP183
DHIS209
DGLU244
DFUD301

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN D 303
ChainResidue
BHOH1470
DASP192
DHOH522

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q9WYP7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22426981","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A9CH28","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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