1ZYZ

Structures of Yeast Ribonucloetide Reductase I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
A	0009263	biological_process	deoxyribonucleotide biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
B	0000166	molecular_function	nucleotide binding
B	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
B	0009263	biological_process	deoxyribonucleotide biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GLY A 889

Chain	Residue
A	THR745

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GLY A 890

Chain	Residue
B	THR745
B	GLN746

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Functional Information from PROSITE/UniProt

site_id	PS00089
Number of Residues	23
Details	RIBORED_LARGE Ribonucleotide reductase large subunit signature. WdtLrkdimkhGVRNsltMApmP

Chain	Residue	Details
A	TRP585-PRO607

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site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ISQkTIINMAADRSVyI

Chain	Residue	Details
A	ILE690-ILE706

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASN426
A	GLU430
B	ASN426
B	GLU430

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Cysteine radical intermediate

Chain	Residue	Details
A	CYS428
B	CYS428

---

site_id	SWS_FT_FI3
Number of Residues	26
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P23921

Chain	Residue	Details
A	LYS5
A	ALA263
A	ASN426
A	GLU430
A	THR608
B	LYS5
B	GLU11
B	THR53
B	ASP57
B	SER202
B	SER217
A	GLU11
B	ASP226
B	LYS243
B	ARG256
B	ALA263
B	ASN426
B	GLU430
B	THR608
A	THR53
A	ASP57
A	SER202
A	SER217
A	ASP226
A	LYS243
A	ARG256

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Important for hydrogen atom transfer => ECO:0000250

Chain	Residue	Details
A	CYS218
A	CYS443
B	CYS218
B	CYS443

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Important for electron transfer => ECO:0000250

Chain	Residue	Details
A	TYR741
A	TYR742
B	TYR741
B	TYR742

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250

Chain	Residue	Details
A	CYS883
A	CYS886
B	CYS883
B	CYS886

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956

Chain	Residue	Details
A	SER227
A	SER837
B	SER227
B	SER837

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21672

Chain	Residue	Details
A	SER816
B	SER816

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	SER887
B	SER887

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site_id	SWS_FT_FI10
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047

Chain	Residue	Details
A	LYS387
A	LYS853
B	LYS387
B	LYS853

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 3r1r

Chain	Residue	Details
A	CYS428
A	ASN426
A	CYS218
A	GLU430
A	CYS443

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 3r1r

Chain	Residue	Details
B	CYS428
B	ASN426
B	CYS218
B	GLU430
B	CYS443

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