2R1R

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TTP A 762

Chain	Residue
A	ASP232
A	SER233
A	LEU234
A	ARG262
A	ILE268
A	ARG269
A	HIS275
B	SER249

---

site_id	AC2
Number of Residues	5
Details	ACTIVE SITE, THE REDOX CENTER, CYS B 225 AND CYS B 462, IN THE OXIDIZED FORM.

Chain	Residue
B	CYS225
B	CYS462
B	CYS439
B	ASN437
B	GLU441

---

site_id	AC3
Number of Residues	5
Details	ACTIVE SITE, THE REDOX CENTER, CYS C 225 AND CYS C 462, IN THE OXIDIZED FORM.

Chain	Residue
C	CYS225
C	CYS462
C	CYS439
C	ASN437
C	GLU441

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TTP B 762

Chain	Residue
A	SER249
B	ASP232
B	SER233
B	LEU234
B	ARG262
B	ILE268
B	ARG269
B	HIS275

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TTP C 762

Chain	Residue
C	ASP232
C	SER233
C	LEU234
C	SER249
C	ARG262
C	ILE268
C	ARG269
C	HIS275

---

site_id	ACT
Number of Residues	5
Details	ACTIVE SITE, THE REDOX CENTER, CYS A 225 AND CYS A 462, IN THE OXIDIZED FORM.

Chain	Residue
A	CYS439
A	ASN437
A	GLU441
A	CYS225
A	CYS462

---

site_id	SE2
Number of Residues	7
Details	RESIDUES INVOLVED IN BINDING DTTP AT THE SPECIFICITY SITE THE SPECIFICITY SITE REGULATES THE SUBSTRATE SPECIFICITY. OTHER EFFECTORS THAT CAN BIND ARE DGTP, DATP AND ATP.

Chain	Residue
B	ASP232
B	LEU234
B	ARG262
B	ILE268
B	HIS275
B	PHE281
B	CYS292

---

site_id	SE3
Number of Residues	7
Details	RESIDUES INVOLVED IN BINDING DTTP AT THE SPECIFICITY SITE THE SPECIFICITY SITE REGULATES THE SUBSTRATE SPECIFICITY. OTHER EFFECTORS THAT CAN BIND ARE DGTP, DATP AND ATP.

Chain	Residue
C	ASP232
C	LEU234
C	ARG262
C	ILE268
C	HIS275
C	PHE281
C	CYS292

---

site_id	SEC
Number of Residues	7
Details	RESIDUES INVOLVED IN BINDING DTTP AT THE SPECIFICITY SITE THE SPECIFICITY SITE REGULATES THE SUBSTRATE SPECIFICITY. OTHER EFFECTORS THAT CAN BIND ARE DGTP, DATP AND ATP.

Chain	Residue
A	ASP232
A	LEU234
A	ARG262
A	ILE268
A	HIS275
A	PHE281
A	CYS292

---

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	270
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	6
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Active site: {"description":"Cysteine radical intermediate"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	27
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	27
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	6
Details	Site: {"description":"Important for hydrogen atom transfer"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Site: {"description":"Important for electron transfer"}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU441
A	CYS462
A	CYS439
A	CYS225
A	ASN437

---

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

Chain	Residue	Details
B	GLU441
B	CYS462
B	CYS439
B	CYS225
B	ASN437

---

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 3r1r

Chain	Residue	Details
C	GLU441
C	CYS462
C	CYS439
C	CYS225
C	ASN437

---

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	TYR730	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
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	MCSA3
Number of Residues
Details	M-CSA 918

Chain

Residue

Details

---

site_id	MCSA4
Number of Residues
Details	M-CSA 918

Chain

Residue

Details

---