Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XO4

RIBONUCLEOTIDE REDUCTASE Y730NH2Y MODIFIED R1 SUBUNIT OF E. COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0005829	cellular_component	cytosol
A	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
A	0006457	biological_process	protein folding
A	0009185	biological_process	ribonucleoside diphosphate metabolic process
A	0009263	biological_process	deoxyribonucleotide biosynthetic process
A	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
A	0015949	biological_process	nucleobase-containing small molecule interconversion
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
A	0044183	molecular_function	protein folding chaperone
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	0005829	cellular_component	cytosol
B	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
B	0006457	biological_process	protein folding
B	0009185	biological_process	ribonucleoside diphosphate metabolic process
B	0009263	biological_process	deoxyribonucleotide biosynthetic process
B	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
B	0015949	biological_process	nucleobase-containing small molecule interconversion
B	0016491	molecular_function	oxidoreductase activity
B	0042802	molecular_function	identical protein binding
B	0044183	molecular_function	protein folding chaperone
C	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
C	0006457	biological_process	protein folding
C	0009185	biological_process	ribonucleoside diphosphate metabolic process
C	0009263	biological_process	deoxyribonucleotide biosynthetic process
C	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
C	0015949	biological_process	nucleobase-containing small molecule interconversion
C	0016491	molecular_function	oxidoreductase activity
C	0042802	molecular_function	identical protein binding
C	0044183	molecular_function	protein folding chaperone

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TRP599-PRO621

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASN437
A	GLU441
B	ASN437
B	GLU441
C	ASN437
C	GLU441

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Cysteine radical intermediate

Chain	Residue	Details
A	CYS439
B	CYS439
C	CYS439

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:9309223, ECO:0007744\|PDB:3R1R

Chain	Residue	Details
A	LYS9
C	GLU15
C	THR55
C	LYS91
A	GLU15
A	THR55
A	LYS91
B	LYS9
B	GLU15
B	THR55
B	LYS91
C	LYS9

site_id	SWS_FT_FI4
Number of Residues	21
Details	BINDING: BINDING => ECO:0000269\|PubMed:9309223, ECO:0007744\|PDB:4R1R

Chain	Residue	Details
A	THR209
B	ARG262
B	ARG269
B	ASN437
B	GLU441
B	GLU623
C	THR209
C	ASP232
C	ARG262
C	ARG269
C	ASN437
A	ASP232
C	GLU441
C	GLU623
A	ARG262
A	ARG269
A	ASN437
A	GLU441
A	GLU623
B	THR209
B	ASP232

site_id	SWS_FT_FI5
Number of Residues	6
Details	SITE: Important for hydrogen atom transfer

Chain	Residue	Details
A	CYS225
A	CYS462
B	CYS225
B	CYS462
C	CYS225
C	CYS462

site_id	SWS_FT_FI6
Number of Residues	6
Details	SITE: Important for electron transfer

Chain	Residue	Details
A	TY2730
A	TYR731
B	TY2730
B	TYR731
C	TY2730
C	TYR731

site_id	SWS_FT_FI7
Number of Residues	6
Details	SITE: Interacts with thioredoxin/glutaredoxin

Chain	Residue	Details
A	CYS754
A	CYS759
B	CYS754
B	CYS759
C	CYS754
C	CYS759

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	LYS283
B	LYS283
C	LYS283

Catalytic Information from CSA

site_id	MCSA1
Number of Residues
Details	M-CSA 918

Chain	Residue	Details
A	CYS225	proton donor
A	ASN437
A	CYS439	hydrogen radical acceptor, hydrogen radical donor, single electron acceptor
A	GLU441	proton acceptor
A	CYS462
A	TY2730	pi-pi interaction, single electron relay
A	TYR731	pi-pi interaction, single electron relay

site_id	MCSA2
Number of Residues
Details	M-CSA 918

Chain	Residue	Details
B	CYS225	proton donor
B	ASN437
B	CYS439	hydrogen radical acceptor, hydrogen radical donor, single electron acceptor
B	GLU441	proton acceptor
B	CYS462
B	TY2730	pi-pi interaction, single electron relay
B	TYR731	pi-pi interaction, single electron relay

site_id	MCSA3
Number of Residues
Details	M-CSA 918

Chain	Residue	Details
C	CYS225	proton donor
C	ASN437
C	CYS439	hydrogen radical acceptor, hydrogen radical donor, single electron acceptor
C	GLU441	proton acceptor
C	CYS462
C	TY2730	pi-pi interaction, single electron relay
C	TYR731	pi-pi interaction, single electron relay

site_id	MCSA4
Number of Residues
Details	M-CSA 918

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)