5YFW

Crystal structure of ribose-1,5-bisphosphate isomerase mutant D204N from Pyrococcus horikoshii OT3 in complex with ribose-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	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 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

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

Chain	Residue	Details
A	ASN204
B	ASN204
C	ASN204

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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

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