5YFJ

Crystal structure of ribose-1,5-bisphosphate isomerase from Pyrococcus horikoshii OT3 in complex with ribulose-1,5-bisphosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016853	molecular_function	isomerase activity
A	0019323	biological_process	pentose catabolic process
A	0043917	molecular_function	ribose 1,5-bisphosphate isomerase activity
A	0044237	biological_process	cellular metabolic process
A	0044249	biological_process	cellular biosynthetic process
B	0016853	molecular_function	isomerase activity
B	0019323	biological_process	pentose catabolic process
B	0043917	molecular_function	ribose 1,5-bisphosphate isomerase activity
B	0044237	biological_process	cellular metabolic process
B	0044249	biological_process	cellular biosynthetic process
C	0016853	molecular_function	isomerase activity
C	0019323	biological_process	pentose catabolic process
C	0043917	molecular_function	ribose 1,5-bisphosphate isomerase activity
C	0044237	biological_process	cellular metabolic process
C	0044249	biological_process	cellular biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue RUB A 401

Chain	Residue
A	MET19
A	ALA139
A	GLN166
A	ALA203
A	ASP204
A	ASN214
A	LYS215
A	LYS240
A	HOH542
A	HOH546
A	HOH552
A	ARG22
A	HOH555
A	HOH559
A	HOH583
A	GLY23
A	ALA24
A	GLY25
A	ARG65
A	CYS135
A	SER137
A	LYS138

---

site_id	AC2
Number of Residues	6
Details	binding site for residue K A 402

Chain	Residue
A	MET193
A	LYS194
A	THR196
A	VAL230
A	HOH591
A	HOH646

---

site_id	AC3
Number of Residues	1
Details	binding site for residue CL A 403

Chain	Residue
A	VAL251

---

site_id	AC4
Number of Residues	5
Details	binding site for residue PEG A 404

Chain	Residue
A	PRO258
A	LEU267
A	LYS272
A	GLU275
A	VAL276

---

site_id	AC5
Number of Residues	2
Details	binding site for residue MPD A 405

Chain	Residue
A	HOH505
B	HOH664

---

site_id	AC6
Number of Residues	22
Details	binding site for residue RUB B 401

Chain	Residue
B	MET19
B	ARG22
B	GLY23
B	ALA24
B	GLY25
B	ARG65
B	CYS135
B	SER137
B	LYS138
B	ALA139
B	GLN166
B	ALA203
B	ASP204
B	ASN214
B	LYS215
B	LYS240
B	HOH506
B	HOH520
B	HOH535
B	HOH541
B	HOH549
B	HOH554

---

site_id	AC7
Number of Residues	6
Details	binding site for residue K B 402

Chain	Residue
B	MET193
B	LYS194
B	THR196
B	VAL230
B	HOH631
B	HOH636

---

site_id	AC8
Number of Residues	2
Details	binding site for residue CL B 403

Chain	Residue
B	LEU250
B	VAL251

---

site_id	AC9
Number of Residues	4
Details	binding site for residue PEG B 404

Chain	Residue
B	TYR62
B	PRO66
B	GLU252
B	HOH555

---

site_id	AD1
Number of Residues	22
Details	binding site for residue RUB C 401

Chain	Residue
C	MET19
C	ARG22
C	GLY23
C	ALA24
C	GLY25
C	ARG65
C	CYS135
C	SER137
C	LYS138
C	ALA139
C	GLN166
C	ALA203
C	ASP204
C	ASN214
C	LYS215
C	LYS240
C	HOH511
C	HOH515
C	HOH517
C	HOH523
C	HOH542
C	HOH563

---

site_id	AD2
Number of Residues	6
Details	binding site for residue K C 402

Chain	Residue
C	MET193
C	LYS194
C	THR196
C	VAL230
C	HOH586
C	HOH605

---

site_id	AD3
Number of Residues	1
Details	binding site for residue CL C 403

Chain	Residue
C	VAL251

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230

Chain	Residue	Details
A	CYS135
B	CYS135
C	CYS135

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02230

Chain	Residue	Details
A	ASP204
B	ASP204
C	ASP204

---

site_id	SWS_FT_FI3
Number of Residues	15
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02230

Chain	Residue	Details
A	ARG22
B	LYS240
C	ARG22
C	ARG65
C	SER137
C	ASN214
C	LYS240
A	ARG65
A	SER137
A	ASN214
A	LYS240
B	ARG22
B	ARG65
B	SER137
B	ASN214

---