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6OTU

Crystal structure of a glucose-6-phosphate isomerase from Chlamydia trachomatis D/UW-3/Cx

Functional Information from GO Data
ChainGOidnamespacecontents
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue ACT A 601
ChainResidue
ATHR47
AGLN454
ALEU524

site_idAC2
Number of Residues2
Detailsbinding site for residue ACT A 602
ChainResidue
AGLY205
AHOH701

site_idAC3
Number of Residues1
Detailsbinding site for residue ACT A 603
ChainResidue
ASER410

site_idAC4
Number of Residues19
Detailsbinding site for residue G6Q A 604
ChainResidue
ASER152
ASER202
ALYS203
ASER204
ATHR207
AGLY260
AARG261
AGLN343
AGLU347
AHIS378
AGLN486
ALYS493
AHOH705
AHOH739
AHOH790
AHOH850
AILE149
AGLY150
AGLY151

Functional Information from PROSITE/UniProt
site_idPS00174
Number of Residues18
DetailsP_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GfCWginsFDQeGVSlgK
ChainResidueDetails
AGLY476-LYS493

site_idPS00765
Number of Residues14
DetailsP_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DsIGGRFSAtSMVG
ChainResidueDetails
AASP256-GLY269

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건을2024-04-17부터공개중

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