1JHB

HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0015036	molecular_function	disulfide oxidoreductase activity
A	0015038	molecular_function	glutathione disulfide oxidoreductase activity
A	0015949	biological_process	nucleobase-containing small molecule interconversion
A	0017080	molecular_function	sodium channel regulator activity
A	0045838	biological_process	positive regulation of membrane potential
A	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AVE
Number of Residues	2
Details	ACTIVE SITE.

Chain	Residue
A	CYS23
A	CYS26

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Functional Information from PROSITE/UniProt

site_id	PS00195
Number of Residues	17
Details	GLUTAREDOXIN_1 Glutaredoxin active site. VFikptCPYCrrAqeiL

Chain	Residue	Details
A	VAL17-LEU33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	103
Details	Domain: {"description":"Glutaredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00686","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9QUH0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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