Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8VHQ

Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
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	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
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	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
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
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
D	0006457	biological_process	protein folding
D	0009185	biological_process	ribonucleoside diphosphate metabolic process
D	0009263	biological_process	deoxyribonucleotide biosynthetic process
D	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
D	0015949	biological_process	nucleobase-containing small molecule interconversion
D	0016491	molecular_function	oxidoreductase activity
D	0042802	molecular_function	identical protein binding
D	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	360
Details	Domain: {"description":"ATP-cone","evidences":[{"source":"PROSITE-ProRule","id":"PRU00492","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Cysteine radical intermediate"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9309223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R1R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9309223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R1R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Site: {"description":"Important for hydrogen atom transfer"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Site: {"description":"Important for electron transfer"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
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	TYR730	pi-pi interaction, single electron relay
A	TYR731	pi-pi interaction, single electron relay

site_id	MCSA2
Number of Residues	7
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	TYR730	pi-pi interaction, single electron relay
B	TYR731	pi-pi interaction, single electron relay

site_id	MCSA3
Number of Residues	7
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	TYR730	pi-pi interaction, single electron relay
C	TYR731	pi-pi interaction, single electron relay

site_id	MCSA4
Number of Residues	7
Details	M-CSA 918

Chain	Residue	Details
D	CYS225	proton donor
D	ASN437
D	CYS439	hydrogen radical acceptor, hydrogen radical donor, single electron acceptor
D	GLU441	proton acceptor
D	CYS462
D	TYR730	pi-pi interaction, single electron relay
D	TYR731	pi-pi interaction, single electron relay

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