Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6AUI

Human ribonucleotide reductase large subunit (alpha) with dATP and CDP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000731	biological_process	DNA synthesis involved in DNA repair
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	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
A	0006264	biological_process	mitochondrial DNA replication
A	0006281	biological_process	DNA repair
A	0009185	biological_process	ribonucleoside diphosphate metabolic process
A	0009263	biological_process	deoxyribonucleotide biosynthetic process
A	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
A	0010971	biological_process	positive regulation of G2/M transition of mitotic cell cycle
A	0016491	molecular_function	oxidoreductase activity
A	0017076	molecular_function	purine nucleotide binding
A	0036175	molecular_function	ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor
A	0042802	molecular_function	identical protein binding
A	0051290	biological_process	protein heterotetramerization
A	0061731	molecular_function	ribonucleoside-diphosphate reductase activity
A	0070318	biological_process	positive regulation of G0 to G1 transition
A	0097718	molecular_function	disordered domain specific binding
A	1900087	biological_process	positive regulation of G1/S transition of mitotic cell cycle
B	0000166	molecular_function	nucleotide binding
B	0000731	biological_process	DNA synthesis involved in DNA repair
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	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
B	0006264	biological_process	mitochondrial DNA replication
B	0006281	biological_process	DNA repair
B	0009185	biological_process	ribonucleoside diphosphate metabolic process
B	0009263	biological_process	deoxyribonucleotide biosynthetic process
B	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
B	0010971	biological_process	positive regulation of G2/M transition of mitotic cell cycle
B	0016491	molecular_function	oxidoreductase activity
B	0017076	molecular_function	purine nucleotide binding
B	0036175	molecular_function	ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor
B	0042802	molecular_function	identical protein binding
B	0051290	biological_process	protein heterotetramerization
B	0061731	molecular_function	ribonucleoside-diphosphate reductase activity
B	0070318	biological_process	positive regulation of G0 to G1 transition
B	0097718	molecular_function	disordered domain specific binding
B	1900087	biological_process	positive regulation of G1/S transition of mitotic cell cycle
C	0000166	molecular_function	nucleotide binding
C	0000731	biological_process	DNA synthesis involved in DNA repair
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	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
C	0006264	biological_process	mitochondrial DNA replication
C	0006281	biological_process	DNA repair
C	0009185	biological_process	ribonucleoside diphosphate metabolic process
C	0009263	biological_process	deoxyribonucleotide biosynthetic process
C	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
C	0010971	biological_process	positive regulation of G2/M transition of mitotic cell cycle
C	0016491	molecular_function	oxidoreductase activity
C	0017076	molecular_function	purine nucleotide binding
C	0036175	molecular_function	ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor
C	0042802	molecular_function	identical protein binding
C	0051290	biological_process	protein heterotetramerization
C	0061731	molecular_function	ribonucleoside-diphosphate reductase activity
C	0070318	biological_process	positive regulation of G0 to G1 transition
C	0097718	molecular_function	disordered domain specific binding
C	1900087	biological_process	positive regulation of G1/S transition of mitotic cell cycle
D	0000166	molecular_function	nucleotide binding
D	0000731	biological_process	DNA synthesis involved in DNA repair
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	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
D	0006264	biological_process	mitochondrial DNA replication
D	0006281	biological_process	DNA repair
D	0009185	biological_process	ribonucleoside diphosphate metabolic process
D	0009263	biological_process	deoxyribonucleotide biosynthetic process
D	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
D	0010971	biological_process	positive regulation of G2/M transition of mitotic cell cycle
D	0016491	molecular_function	oxidoreductase activity
D	0017076	molecular_function	purine nucleotide binding
D	0036175	molecular_function	ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor
D	0042802	molecular_function	identical protein binding
D	0051290	biological_process	protein heterotetramerization
D	0061731	molecular_function	ribonucleoside-diphosphate reductase activity
D	0070318	biological_process	positive regulation of G0 to G1 transition
D	0097718	molecular_function	disordered domain specific binding
D	1900087	biological_process	positive regulation of G1/S transition of mitotic cell cycle
E	0000166	molecular_function	nucleotide binding
E	0000731	biological_process	DNA synthesis involved in DNA repair
E	0003824	molecular_function	catalytic activity
E	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005829	cellular_component	cytosol
E	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
E	0006264	biological_process	mitochondrial DNA replication
E	0006281	biological_process	DNA repair
E	0009185	biological_process	ribonucleoside diphosphate metabolic process
E	0009263	biological_process	deoxyribonucleotide biosynthetic process
E	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
E	0010971	biological_process	positive regulation of G2/M transition of mitotic cell cycle
E	0016491	molecular_function	oxidoreductase activity
E	0017076	molecular_function	purine nucleotide binding
E	0036175	molecular_function	ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor
E	0042802	molecular_function	identical protein binding
E	0051290	biological_process	protein heterotetramerization
E	0061731	molecular_function	ribonucleoside-diphosphate reductase activity
E	0070318	biological_process	positive regulation of G0 to G1 transition
E	0097718	molecular_function	disordered domain specific binding
E	1900087	biological_process	positive regulation of G1/S transition of mitotic cell cycle
F	0000166	molecular_function	nucleotide binding
F	0000731	biological_process	DNA synthesis involved in DNA repair
F	0003824	molecular_function	catalytic activity
F	0004748	molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005829	cellular_component	cytosol
F	0005971	cellular_component	ribonucleoside-diphosphate reductase complex
F	0006264	biological_process	mitochondrial DNA replication
F	0006281	biological_process	DNA repair
F	0009185	biological_process	ribonucleoside diphosphate metabolic process
F	0009263	biological_process	deoxyribonucleotide biosynthetic process
F	0009265	biological_process	2'-deoxyribonucleotide biosynthetic process
F	0010971	biological_process	positive regulation of G2/M transition of mitotic cell cycle
F	0016491	molecular_function	oxidoreductase activity
F	0017076	molecular_function	purine nucleotide binding
F	0036175	molecular_function	ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor
F	0042802	molecular_function	identical protein binding
F	0051290	biological_process	protein heterotetramerization
F	0061731	molecular_function	ribonucleoside-diphosphate reductase activity
F	0070318	biological_process	positive regulation of G0 to G1 transition
F	0097718	molecular_function	disordered domain specific binding
F	1900087	biological_process	positive regulation of G1/S transition of mitotic cell cycle

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue DTP A 801

Chain	Residue
A	VAL3
A	ASP57
A	LYS88
A	MG802
A	HOH902
A	HOH905
A	HOH906
A	LYS5
A	ARG6
A	GLU11
A	ARG12
A	VAL13
A	MET14
A	ARG21
A	THR53

site_id	AC2
Number of Residues	4
Details	binding site for residue MG A 802

Chain	Residue
A	DTP801
A	HOH902
A	HOH905
A	HOH906

site_id	AC3
Number of Residues	13
Details	binding site for residue DTP A 803

Chain	Residue
A	ASP226
A	SER227
A	ARG256
A	ILE262
A	ALA263
A	GLY264
A	MG804
A	HOH901
A	HOH903
A	HOH904
B	LYS243
B	ASP287
B	GLY289

site_id	AC4
Number of Residues	4
Details	binding site for residue MG A 804

Chain	Residue
A	DTP803
A	HOH901
A	HOH903
A	HOH904

site_id	AC5
Number of Residues	15
Details	binding site for residue CDP A 805

Chain	Residue
A	SER202
A	SER217
A	CYS218
A	GLY247
A	GLN288
A	ARG293
A	ASN427
A	CYS429
A	GLU431
A	LEU446
A	PRO603
A	THR604
A	ALA605
A	SER606
A	THR607

site_id	AC6
Number of Residues	16
Details	binding site for residue DTP B 801

Chain	Residue
B	VAL3
B	LYS5
B	ARG6
B	GLU11
B	ARG12
B	VAL13
B	MET14
B	ARG21
B	THR53
B	LEU56
B	ASP57
B	LYS88
B	MG802
B	HOH902
B	HOH904
B	HOH905

site_id	AC7
Number of Residues	4
Details	binding site for residue MG B 802

Chain	Residue
B	DTP801
B	HOH902
B	HOH904
B	HOH905

site_id	AC8
Number of Residues	12
Details	binding site for residue DTP B 803

Chain	Residue
A	LYS243
A	ASP287
A	GLY289
B	ASP226
B	SER227
B	ARG256
B	ALA263
B	GLY264
B	MG804
B	HOH901
B	HOH903
B	HOH906

site_id	AC9
Number of Residues	4
Details	binding site for residue MG B 804

Chain	Residue
B	DTP803
B	HOH901
B	HOH903
B	HOH906

site_id	AD1
Number of Residues	15
Details	binding site for residue CDP B 805

Chain	Residue
B	ALA605
B	SER606
B	THR607
B	SER202
B	SER217
B	CYS218
B	GLY247
B	GLN288
B	ARG293
B	ASN427
B	CYS429
B	GLU431
B	LEU446
B	PRO603
B	THR604

site_id	AD2
Number of Residues	16
Details	binding site for residue DTP C 801

Chain	Residue
C	VAL3
C	LYS5
C	ARG6
C	GLU11
C	ARG12
C	VAL13
C	MET14
C	ARG21
C	THR53
C	LEU56
C	ASP57
C	LYS88
C	MG802
C	HOH902
C	HOH905
C	HOH906

site_id	AD3
Number of Residues	4
Details	binding site for residue MG C 802

Chain	Residue
C	DTP801
C	HOH902
C	HOH905
C	HOH906

site_id	AD4
Number of Residues	13
Details	binding site for residue DTP C 803

Chain	Residue
C	ASP226
C	SER227
C	ILE228
C	ARG256
C	ALA263
C	GLY264
C	MG804
C	HOH901
C	HOH903
C	HOH904
D	LYS243
D	ASP287
D	GLY289

site_id	AD5
Number of Residues	4
Details	binding site for residue MG C 804

Chain	Residue
C	DTP803
C	HOH901
C	HOH903
C	HOH904

site_id	AD6
Number of Residues	15
Details	binding site for residue CDP C 805

Chain	Residue
C	SER202
C	SER217
C	CYS218
C	GLY247
C	GLN288
C	ARG293
C	ASN427
C	CYS429
C	GLU431
C	LEU446
C	PRO603
C	THR604
C	ALA605
C	SER606
C	THR607

site_id	AD7
Number of Residues	16
Details	binding site for residue DTP D 801

Chain	Residue
D	VAL3
D	LYS5
D	ARG6
D	ARG12
D	VAL13
D	MET14
D	ILE18
D	ARG21
D	THR53
D	LEU56
D	ASP57
D	LYS88
D	MG802
D	HOH902
D	HOH905
D	HOH906

site_id	AD8
Number of Residues	4
Details	binding site for residue MG D 802

Chain	Residue
D	DTP801
D	HOH902
D	HOH905
D	HOH906

site_id	AD9
Number of Residues	12
Details	binding site for residue DTP D 803

Chain	Residue
C	LYS243
C	ASP287
C	GLY289
D	ASP226
D	SER227
D	ARG256
D	ALA263
D	GLY264
D	MG804
D	HOH901
D	HOH903
D	HOH904

site_id	AE1
Number of Residues	4
Details	binding site for residue MG D 804

Chain	Residue
D	DTP803
D	HOH901
D	HOH903
D	HOH904

site_id	AE2
Number of Residues	15
Details	binding site for residue CDP D 805

Chain	Residue
D	SER202
D	SER217
D	CYS218
D	GLY247
D	GLN288
D	ARG293
D	ASN427
D	CYS429
D	GLU431
D	LEU446
D	PRO603
D	THR604
D	ALA605
D	SER606
D	THR607

site_id	AE3
Number of Residues	15
Details	binding site for residue DTP E 801

Chain	Residue
E	VAL3
E	LYS5
E	ARG6
E	GLU11
E	ARG12
E	VAL13
E	MET14
E	ARG21
E	THR53
E	ASP57
E	LYS88
E	MG802
E	HOH902
E	HOH903
E	HOH906

site_id	AE4
Number of Residues	4
Details	binding site for residue MG E 802

Chain	Residue
E	DTP801
E	HOH902
E	HOH903
E	HOH906

site_id	AE5
Number of Residues	13
Details	binding site for residue DTP E 803

Chain	Residue
E	ASP226
E	SER227
E	ARG256
E	ILE262
E	ALA263
E	GLY264
E	MG804
E	HOH901
E	HOH904
E	HOH905
F	LYS243
F	ASP287
F	GLY289

site_id	AE6
Number of Residues	4
Details	binding site for residue MG E 804

Chain	Residue
E	DTP803
E	HOH901
E	HOH904
E	HOH905

site_id	AE7
Number of Residues	14
Details	binding site for residue CDP E 805

Chain	Residue
E	SER202
E	SER217
E	GLY247
E	GLN288
E	ARG293
E	ASN427
E	CYS429
E	GLU431
E	LEU446
E	PRO603
E	THR604
E	ALA605
E	SER606
E	THR607

site_id	AE8
Number of Residues	15
Details	binding site for residue DTP F 801

Chain	Residue
F	VAL3
F	LYS5
F	ARG6
F	ARG12
F	VAL13
F	MET14
F	ARG21
F	THR53
F	LEU56
F	ASP57
F	LYS88
F	MG802
F	HOH903
F	HOH904
F	HOH906

site_id	AE9
Number of Residues	4
Details	binding site for residue MG F 802

Chain	Residue
F	DTP801
F	HOH903
F	HOH904
F	HOH906

site_id	AF1
Number of Residues	14
Details	binding site for residue DTP F 803

Chain	Residue
E	LYS243
E	ASP287
E	GLY289
F	ASP226
F	SER227
F	ARG256
F	TYR261
F	ILE262
F	ALA263
F	GLY264
F	MG804
F	HOH901
F	HOH902
F	HOH905

site_id	AF2
Number of Residues	4
Details	binding site for residue MG F 804

Chain	Residue
F	DTP803
F	HOH901
F	HOH902
F	HOH905

site_id	AF3
Number of Residues	15
Details	binding site for residue CDP F 805

Chain	Residue
F	SER202
F	SER217
F	CYS218
F	GLY247
F	GLN288
F	ARG293
F	ASN427
F	CYS429
F	GLU431
F	LEU446
F	PRO603
F	THR604
F	ALA605
F	SER606
F	THR607

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TRP581-PRO603

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	546
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	12
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Active site: {"description":"Cysteine radical intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	84
Details	Binding site: {"evidences":[{"source":"PDB","id":"3HNE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"PDB","id":"3HND","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Site: {"description":"Important for hydrogen atom transfer","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Site: {"description":"Important for electron transfer","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)