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6QUF

Protein crystallization by ionic liquid hydrogel support: reference crystal of glucose isomerase grown on standard silanized glass

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 Residues5
Detailsbinding site for residue MN A 401
ChainResidue
AGLU217
AHIS220
AASP255
AASP257
AHOH798

site_idAC2
Number of Residues5
Detailsbinding site for residue MN A 402
ChainResidue
AGOL404
AGLU181
AGLU217
AASP245
AASP287

site_idAC3
Number of Residues13
Detailsbinding site for residue GOL A 403
ChainResidue
APRO25
APRO25
ATYR254
AASP255
AGLN256
ALYS289
AHOH527
AHOH536
AHOH539
AHOH548
AHOH565
AHOH844
AHOH882

site_idAC4
Number of Residues10
Detailsbinding site for residue GOL A 404
ChainResidue
AHIS54
ATRP137
AGLU181
AGLU217
AHIS220
AASP245
AASP287
AMN402
AHOH691
AHOH698

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 A 405
ChainResidue
AARG23
AASP28
AALA29
AHOH501
AHOH516
AHOH779
AHOH811

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 406
ChainResidue
AGLY19
ATRP20
AGLN21
AARG23
AHOH503
AHOH886

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AHIS54

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP57

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AGLU181
AGLU217
AHIS220
AASP245
AASP255
AASP257
AASP287

218853

PDB entries from 2024-04-24

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