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1XIJ

MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE

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
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE THE A 389
ChainResidue
ATRP16
AHOH408
AHOH413
AHOH565
AHOH585
AHIS54
ATRP137
AGLU181
AGLU217
AHIS220
AASP245
AASP287
AMN391

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 391
ChainResidue
AGLU181
AGLU217
AASP245
AASP287
ATHE389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AASP55

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ALEU58

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING:
ChainResidueDetails
APRO182
AVAL218
AGLU221
ALEU246
AGLN256
ALEU258
APHE288

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
ALYS183
AHIS220
AASP255

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AARG292

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AGLU181
AHIS54
ALYS183
AASP57

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PDB entries from 2024-05-01

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