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1MUW

The 0.86 Angstrom Structure of 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
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MN A 451
ChainResidue
AGLU216
AHIS219
AASN246
AASP254
AASP256
AOH455
AHOH589
AHOH788

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 452
ChainResidue
AGLU216
AASP244
AASP286
AHOH788
AGLU180

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 453
ChainResidue
AASP162
AGLU206
AARG207
ATYR211
AHOH829

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 454
ChainResidue
APRO35
ALEU57
AHIS70
AHOH539

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OH A 455
ChainResidue
AGLU216
AHIS219
AASP254
AASP256
AASP286
AMN451
AHOH788

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP54
ALEU57

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
APRO181
AVAL217
AGLU220
ALEU245
AGLN255
ALEU257
APHE287

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

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AARG291

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1de6
ChainResidueDetails
AGLU180
ALYS182
AASP56
AHIS53

224572

PDB entries from 2024-09-04

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