1H9B

ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004345	molecular_function	glucose-6-phosphate dehydrogenase activity
A	0005829	cellular_component	cytosol
A	0006006	biological_process	glucose metabolic process
A	0006098	biological_process	pentose-phosphate shunt
A	0009051	biological_process	pentose-phosphate shunt, oxidative branch
A	0016491	molecular_function	oxidoreductase activity
A	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
A	0050661	molecular_function	NADP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 610

Chain	Residue
A	HIS178
A	TYR179
A	LYS182
A	LYS343
A	ASP374

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Functional Information from PROSITE/UniProt

site_id	PS00069
Number of Residues	7
Details	G6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE

Chain	Residue	Details
A	ASP177-GLU183

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:9485426

Chain	Residue	Details
A	THR241

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11320304, ECO:0000269|PubMed:9485426

Chain	Residue	Details
A	GLY13
A	GLN47
A	VAL86

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11320304

Chain	Residue	Details
A	PRO149

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site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:11106478

Chain	Residue	Details
A	TYR179
A	GLU183
A	VAL217
A	MET236
A	ARG339
A	GLN344

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1dpg

Chain	Residue	Details
A	ASP177
A	HIS240

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 843

Chain	Residue	Details
A	HIS178	modifies pKa
A	TYR179	transition state stabiliser
A	THR241	proton acceptor, proton donor

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