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1XLL

MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0009045molecular_functionxylose isomerase activity
A0016853molecular_functionisomerase activity
A0042732biological_processD-xylose metabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0009045molecular_functionxylose isomerase activity
B0016853molecular_functionisomerase activity
B0042732biological_processD-xylose metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 398
ChainResidue
AGLU216
AHIS219
AASP254
AASP256
AHOH503
AHOH633

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 399
ChainResidue
AASP292
AGLU180
AGLU216
AASP244

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 398
ChainResidue
BGLU216
BHIS219
BASP254
BASP256
BHOH508

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 399
ChainResidue
BGLU180
BGLU216
BASP244
BASP292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2319597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AASP254
ALYS182
AHIS219

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
BASP254
BLYS182
BHIS219

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AARG297

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
BARG297

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AGLU180
ALYS182
AASP56
AHIS53

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
BGLU180
BLYS182
BASP56
BHIS53

site_idMCSA1
Number of Residues11
DetailsM-CSA 308
ChainResidueDetails
AHIS53activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP256metal ligand
AASP292activator, attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor
AASP56activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AMET87polar interaction, steric role
AGLU180metal ligand
ALYS182electrostatic stabiliser, hydrogen bond donor, proton donor
AGLU216metal ligand
AHIS219metal ligand
AASP244metal ligand
AASP254metal ligand

site_idMCSA2
Number of Residues11
DetailsM-CSA 308
ChainResidueDetails
BHIS53activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASP256metal ligand
BASP292activator, attractive charge-charge interaction, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor
BASP56activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BMET87polar interaction, steric role
BGLU180metal ligand
BLYS182electrostatic stabiliser, hydrogen bond donor, proton donor
BGLU216metal ligand
BHIS219metal ligand
BASP244metal ligand
BASP254metal ligand

238895

PDB entries from 2025-07-16

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