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1XLM

D254E, D256E MUTANT OF D-XYLOSE ISOMERASE COMPLEXED WITH AL3 AND XYLITOL

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_idCTA
Number of Residues13
DetailsCATALYTIC SITE.
ChainResidue
BTHR16
ALEU245
AGLN255
ALEU257
AGLY287
BASP54
BLEU57
BSER94
BGLY137
BPRO181
BPRO183
BPRO186
AGLU220

site_idCTB
Number of Residues13
DetailsCATALYTIC SITE.
ChainResidue
BTHR16
BASP54
BLEU57
BSER94
BGLY137
BPRO181
BPRO183
BPRO186
BGLU220
BLEU245
BGLN255
BLEU257
BGLY287

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 Residues1
DetailsAnnotated By Reference To The Literature 1qum
ChainResidueDetails
AARG297

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qum
ChainResidueDetails
BARG297

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qum
ChainResidueDetails
AGLU180
ALYS182
AASP56
AHIS53

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qum
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
AGLU256metal 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
AGLU254metal ligand

site_idMCSA2
Number of Residues11
DetailsM-CSA 308
ChainResidueDetails
BHIS53activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLU256metal 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
BGLU254metal ligand

246031

PDB entries from 2025-12-10

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