3R1R

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY 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	11
Details	BINDING SITE FOR RESIDUE ATP A 762

Chain	Residue
A	LYS9
A	GLU15
A	ARG16
A	ILE17
A	ASN18
A	LYS21
A	ILE22
A	VAL25
A	THR55
A	HIS59
A	LYS91

---

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	11
Details	BINDING SITE FOR RESIDUE ATP B 762

Chain	Residue
B	LYS9
B	GLU15
B	ARG16
B	ILE17
B	ASN18
B	LYS21
B	ILE22
B	VAL25
B	THR55
B	HIS59
B	LYS91

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ATP C 762

Chain	Residue
C	LYS9
C	GLU15
C	ARG16
C	ILE17
C	ASN18
C	LYS21
C	ILE22
C	VAL25
C	THR55
C	HIS59
C	LYS91

---

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	CYS225
A	CYS462
A	CYS439
A	ASN437
A	GLU441

---

site_id	AF2
Number of Residues	11
Details	RESIDUES INVOLVED IN BINDING AMPPNP (ATP) AT THE ACTIVITY SITE. THE ACTIVITY SITE REGULATES THE ACTIVITY. EFFECTORS THAT CAN BIND ARE ATP (ACTIVATOR) OR DATP (INHIBITOR).

Chain	Residue
B	VAL7
B	LYS9
B	ARG10
B	GLU15
B	LYS21
B	ILE22
B	THR55
B	ILE58
B	HIS59
B	HIS88
B	LYS91

---

site_id	AF3
Number of Residues	11
Details	RESIDUES INVOLVED IN BINDING AMPPNP (ATP) AT THE ACTIVITY SITE. THE ACTIVITY SITE REGULATES THE ACTIVITY. EFFECTORS THAT CAN BIND ARE ATP (ACTIVATOR) OR DATP (INHIBITOR).

Chain	Residue
C	VAL7
C	LYS9
C	ARG10
C	GLU15
C	LYS21
C	ILE22
C	THR55
C	ILE58
C	HIS59
C	HIS88
C	LYS91

---

site_id	AFF
Number of Residues	11
Details	RESIDUES INVOLVED IN BINDING AMPPNP (ATP) AT THE ACTIVITY SITE. THE ACTIVITY SITE REGULATES THE ACTIVITY. EFFECTORS THAT CAN BIND ARE ATP (ACTIVATOR) OR DATP (INHIBITOR).

Chain	Residue
A	VAL7
A	HIS88
A	LYS91
A	LYS9
A	ARG10
A	GLU15
A	LYS21
A	ILE22
A	THR55
A	ILE58
A	HIS59

---

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

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

---

site_id	CSA2
Number of Residues	5
Details

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

---

site_id	CSA3
Number of Residues	5
Details

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

---