5YFU

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016853	molecular_function	isomerase activity
A	0019323	biological_process	pentose catabolic process
A	0019509	biological_process	L-methionine salvage from methylthioadenosine
A	0043917	molecular_function	ribose 1,5-bisphosphate isomerase activity
A	0046523	molecular_function	S-methyl-5-thioribose-1-phosphate isomerase activity
B	0016853	molecular_function	isomerase activity
B	0019323	biological_process	pentose catabolic process
B	0019509	biological_process	L-methionine salvage from methylthioadenosine
B	0043917	molecular_function	ribose 1,5-bisphosphate isomerase activity
B	0046523	molecular_function	S-methyl-5-thioribose-1-phosphate isomerase activity
C	0016853	molecular_function	isomerase activity
C	0019323	biological_process	pentose catabolic process
C	0019509	biological_process	L-methionine salvage from methylthioadenosine
C	0043917	molecular_function	ribose 1,5-bisphosphate isomerase activity
C	0046523	molecular_function	S-methyl-5-thioribose-1-phosphate isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
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	PHE281
A	HOH526
A	HOH545
A	ARG22
A	HOH557
A	HOH571
A	GLY23
A	ALA24
A	GLY25
A	ARG65
A	CYS135
A	SER137
A	LYS138

---

site_id	AC2
Number of Residues	4
Details	binding site for residue K A 402

Chain	Residue
A	MET193
A	LYS194
A	THR196
A	VAL230

---

site_id	AC3
Number of Residues	18
Details	binding site for residue AMP A 403

Chain	Residue
A	ARG124
A	ARG190
A	LYS194
A	ARG229
A	TRP231
A	ASP290
A	HOH501
A	HOH508
A	HOH510
A	HOH565
B	THR207
B	ASN209
B	ALA211
B	LEU250
B	VAL251
B	VAL283
B	PRO286
B	HOH503

---

site_id	AC4
Number of Residues	2
Details	binding site for residue MPD A 404

Chain	Residue
A	TYR288
B	TYR288

---

site_id	AC5
Number of Residues	20
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	ASP204
B	ASN214
B	LYS215
B	LYS240
B	HOH504
B	HOH508
B	HOH521
B	HOH535
B	HOH558

---

site_id	AC6
Number of Residues	3
Details	binding site for residue K B 402

Chain	Residue
B	MET193
B	LYS194
B	THR196

---

site_id	AC7
Number of Residues	15
Details	binding site for residue AMP B 403

Chain	Residue
B	ARG124
B	ARG229
B	TRP231
B	ASP290
B	HOH501
B	HOH502
B	HOH532
C	ARG190
C	LYS194
C	THR207
C	ASN209
C	ALA211
C	LEU250
C	VAL251
C	VAL283

---

site_id	AC8
Number of Residues	21
Details	binding site for residue RUB C 401

Chain	Residue
C	HOH512
C	HOH514
C	HOH523
C	HOH524
C	HOH528
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

---

site_id	AC9
Number of Residues	5
Details	binding site for residue K C 402

Chain	Residue
C	MET193
C	LYS194
C	THR196
C	VAL230
C	HOH573

---

site_id	AD1
Number of Residues	16
Details	binding site for residue AMP C 403

Chain	Residue
A	THR207
A	ASN209
A	ALA211
A	LEU250
A	VAL251
A	VAL283
A	PRO286
B	ARG190
B	LYS194
C	ARG124
C	ARG229
C	TRP231
C	ASP290
C	HOH501
C	HOH505
C	HOH519

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---