2BH9

X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004345	molecular_function	glucose-6-phosphate dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0005536	molecular_function	D-glucose binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006006	biological_process	glucose metabolic process
A	0006098	biological_process	pentose-phosphate shunt
A	0006629	biological_process	lipid metabolic process
A	0006695	biological_process	cholesterol biosynthetic process
A	0006739	biological_process	NADP+ metabolic process
A	0006740	biological_process	NADPH regeneration
A	0006749	biological_process	glutathione metabolic process
A	0009051	biological_process	pentose-phosphate shunt, oxidative branch
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0010041	biological_process	response to iron(III) ion
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
A	0019322	biological_process	pentose biosynthetic process
A	0021762	biological_process	substantia nigra development
A	0030246	molecular_function	carbohydrate binding
A	0032094	biological_process	response to food
A	0034451	cellular_component	centriolar satellite
A	0034599	biological_process	cellular response to oxidative stress
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043249	biological_process	erythrocyte maturation
A	0043523	biological_process	regulation of neuron apoptotic process
A	0045471	biological_process	response to ethanol
A	0046390	biological_process	ribose phosphate biosynthetic process
A	0050661	molecular_function	NADP binding
A	0051156	biological_process	glucose 6-phosphate metabolic process
A	0061052	biological_process	negative regulation of cell growth involved in cardiac muscle cell development
A	0070062	cellular_component	extracellular exosome
A	1904879	biological_process	positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
A	2000378	biological_process	negative regulation of reactive oxygen species metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAP A 799

Chain	Residue
A	GLY38
A	ASP114
A	ALA141
A	LEU142
A	PRO143
A	TYR147
A	GLU170
A	LYS171
A	HOH2154
A	HOH2155
A	SER40
A	GLY41
A	ASP42
A	LEU43
A	ARG72
A	SER73
A	GLN111
A	TYR112

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAP A 811

Chain	Residue
A	LYS238
A	LYS366
A	ARG370
A	ARG393
A	TYR401
A	LYS403
A	ASP421
A	THR423
A	ARG487
A	ASP493
A	PHE501
A	TYR503
A	TYR507
A	TRP509
A	HOH2152
A	HOH2157
A	HOH2159
A	HOH2161

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A1516

Chain	Residue
A	GLY248
A	TYR249
A	GLU252
A	THR327

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A1517

Chain	Residue
A	PRO467
A	GLN471
A	LEU474
A	HOH2162

---

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	ASP200-GLU206

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P11411","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	21
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10745013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15858258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QKI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BH9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15858258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BH9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15858258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BHL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"24769394","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP200
A	HIS263

---