1EGR

SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005737	cellular_component	cytoplasm
A	0009055	molecular_function	electron transfer activity
A	0009263	biological_process	deoxyribonucleotide biosynthetic process
A	0010134	biological_process	sulfate assimilation via adenylyl sulfate reduction
A	0015035	molecular_function	protein-disulfide reductase activity
A	0015036	molecular_function	disulfide oxidoreductase activity
A	0015038	molecular_function	glutathione disulfide oxidoreductase activity
A	0019153	molecular_function	protein-disulfide reductase (glutathione) activity
A	0019345	biological_process	cysteine biosynthetic process via S-sulfo-L-cysteine
A	0034599	biological_process	cellular response to oxidative stress
A	0045454	biological_process	cell redox homeostasis

Functional Information from PROSITE/UniProt

site_id	PS00195
Number of Residues	16
Details	GLUTAREDOXIN_1 Glutaredoxin active site. IFgrsgCPYCvrAkd.L

Chain	Residue	Details
A	ILE5-LEU20

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: O-AMP-tyrosine; by YdiU => ECO:0000269|PubMed:30270044

Chain	Residue	Details
A	TYR13

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1qfn

Chain	Residue	Details
A	TYR13
A	ARG8
A	GLY10
A	LYS18
A	TYR72

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site_id	MCSA1
Number of Residues	7
Details	M-CSA 792

Chain	Residue	Details
A	ARG8	enhance reactivity, modifies pKa
A	GLY10	electrostatic stabiliser, proton acceptor, proton donor
A	CYS11	electrofuge, electrophile, nucleophile
A	TYR13	electrostatic stabiliser
A	CYS14	nucleophile, proton donor
A	LYS18	enhance reactivity
A	TYR72	electrostatic stabiliser

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