2R87

Crystal structure of PurP from Pyrococcus furiosus complexed with ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0005524	molecular_function	ATP binding
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006188	biological_process	IMP biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0016874	molecular_function	ligase activity
A	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0005524	molecular_function	ATP binding
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006188	biological_process	IMP biosynthetic process
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0016874	molecular_function	ligase activity
B	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0005524	molecular_function	ATP binding
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0006188	biological_process	IMP biosynthetic process
C	0006189	biological_process	'de novo' IMP biosynthetic process
C	0016874	molecular_function	ligase activity
C	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0005524	molecular_function	ATP binding
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0006188	biological_process	IMP biosynthetic process
D	0006189	biological_process	'de novo' IMP biosynthetic process
D	0016874	molecular_function	ligase activity
D	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0005524	molecular_function	ATP binding
E	0006164	biological_process	purine nucleotide biosynthetic process
E	0006188	biological_process	IMP biosynthetic process
E	0006189	biological_process	'de novo' IMP biosynthetic process
E	0016874	molecular_function	ligase activity
E	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0005524	molecular_function	ATP binding
F	0006164	biological_process	purine nucleotide biosynthetic process
F	0006188	biological_process	IMP biosynthetic process
F	0006189	biological_process	'de novo' IMP biosynthetic process
F	0016874	molecular_function	ligase activity
F	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 401

Chain	Residue
A	SER10
A	SER71
C	ARG238
C	SER240
C	HOH505

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 402

Chain	Residue
A	HOH508
A	HOH601
A	HOH602
A	HIS11
A	ARG202
A	ARG287
A	ALA290

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 A 501

Chain	Residue
A	TYR306
A	ARG308

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 401

Chain	Residue
A	ARG238
A	SER240
A	HOH510
B	SER10
B	HIS11
B	SER71

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 B 402

Chain	Residue
B	HIS11
B	ARG202
B	ARG287
B	ALA290
B	HOH571
B	HOH574

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 501

Chain	Residue
B	ARG191
B	ARG308
B	MET318
B	HOH589

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 401

Chain	Residue
B	ARG238
B	SER240
B	HOH540
C	SER10
C	SER71

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 402

Chain	Residue
C	HIS11
C	ARG202
C	ARG287
C	ALA290
C	HOH548

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 500

Chain	Residue
C	ARG105
C	LYS109
C	HOH558
C	HOH569

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 501

Chain	Residue
C	ARG191
C	TYR306
C	ARG308
C	MET318
C	HOH589

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 F 401

Chain	Residue
D	SER10
D	SER71
D	HIS75
F	ARG238
F	SER240
F	HOH504

---

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 D 402

Chain	Residue
D	HIS11
D	ARG202
D	ARG287
D	ALA290
D	HOH546

---

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 D 501

Chain	Residue
D	TYR306
D	ARG308

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 D 401

Chain	Residue
D	ARG238
D	SER240
D	HOH513
E	SER10
E	SER71

---

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 402

Chain	Residue
E	HIS11
E	ARG202
E	ARG287
E	ALA290
E	HOH536

---

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 E 501

Chain	Residue
E	ARG191
E	ARG308

---

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 E 401

Chain	Residue
E	ARG238
E	SER240
E	HOH508
F	SER10
F	SER71
F	HIS75

---

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 402

Chain	Residue
F	HIS11
F	ARG202
F	ARG287
F	ALA290
F	HOH502

---

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 F 501

Chain	Residue
F	ARG191
F	ARG308

---

site_id	CC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP A 400

Chain	Residue
A	PHE282
A	GLU283
A	HOH514
A	HOH553
B	ARG212
A	PRO116
A	ILE130
A	LYS132
A	GLY138
A	GLY139
A	TYR142
A	GLN173
A	GLU174
A	TYR175
A	ARG202
A	GLU204
A	GLU270

---

site_id	CC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP B 400

Chain	Residue
B	PRO116
B	ILE130
B	LYS132
B	LYS137
B	GLY138
B	GLY139
B	TYR142
B	GLN173
B	GLU174
B	TYR175
B	GLU204
B	TYR227
B	GLU270
B	PHE282
B	GLU283
B	HOH564
B	HOH568
C	ARG212

---

site_id	CC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP C 400

Chain	Residue
A	ARG212
C	ILE130
C	LYS132
C	LYS137
C	GLY138
C	GLY139
C	TYR142
C	GLN173
C	GLU174
C	TYR175
C	GLU204
C	GLU270
C	PHE282
C	GLU283
C	HOH522
C	HOH531
C	HOH541

---

site_id	CC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP D 400

Chain	Residue
D	PRO116
D	ILE130
D	LYS132
D	GLY138
D	GLY139
D	TYR142
D	GLN173
D	GLU174
D	TYR175
D	ARG202
D	GLU204
D	GLU270
D	PHE282
D	GLU283
E	ARG212

---

site_id	CC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP E 400

Chain	Residue
E	ILE130
E	LYS132
E	ALA136
E	GLY138
E	GLY139
E	TYR142
E	GLN173
E	GLU174
E	TYR175
E	ARG202
E	GLU204
E	TYR227
E	PHE282
E	GLU283
E	HOH516
F	ARG212

---

site_id	CC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP F 400

Chain	Residue
D	ARG212
F	ARG101
F	ILE130
F	LYS132
F	LYS137
F	GLY138
F	GLY139
F	TYR142
F	GLN173
F	GLU174
F	TYR175
F	TYR182
F	ARG202
F	GLU204
F	GLU270
F	PHE282
F	GLU283

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1482
Details	Domain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_01163","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	114
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01163","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---