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1XYL

THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID

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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AGLU216
AHIS219
AASP254
AASP256
AOH1700

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OH A 1700
ChainResidue
AGLU216
AHIS219
AASP254
AASP256
AMG401
AHOH1275

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 901
ChainResidue
BGLU716
BHIS719
BASP754
BASP756
BOH1800

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OH B 1800
ChainResidue
BGLU716
BASP754
BASP756
BASP786
BMG901
BHOH1120

site_idM1A
Number of Residues4
DetailsMETAL BINDING SITE REPLACED BY THE N-EPSILON AMINO GROUPS OF LYS
ChainResidue
ALYS180
AASP244
AASP286
AGLU216

site_idM1B
Number of Residues4
DetailsMETAL BINDING SITE REPLACED BY THE N-EPSILON AMINO GROUPS OF LYS
ChainResidue
BLYS680
BASP744
BASP786
BGLU716

site_idM2A
Number of Residues6
DetailsMETAL BINDING SITE IN ACTIVE SITE WITH BOUND MG
ChainResidue
AOH1700
AMG401
AGLU216
AHIS219
AASP254
AASP256

site_idM2B
Number of Residues6
DetailsMETAL BINDING SITE IN ACTIVE SITE WITH BOUND MG
ChainResidue
BMG901
BGLU716
BHIS719
BASP754
BASP756
BOH1800

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
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
BHIS719
BASP754
BLYS682

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AARG291

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
BARG791

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
ALYS180
ALYS182
AASP56
AHIS53

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
BHIS553
BLYS680
BLYS682
BASP556

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PDB entries from 2025-12-31

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