3VSY

High-resolution crystal structure of wild-type KSI in the apo form at neutral pH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004769	molecular_function	steroid Delta-isomerase activity
A	0006629	biological_process	lipid metabolic process
A	0008202	biological_process	steroid metabolic process
A	0016853	molecular_function	isomerase activity
B	0004769	molecular_function	steroid Delta-isomerase activity
B	0006629	biological_process	lipid metabolic process
B	0008202	biological_process	steroid metabolic process
B	0016853	molecular_function	isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 201

Chain	Residue
B	ARG106
B	THR115
B	GLN117
B	HOH326

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 202

Chain	Residue
B	ARG106
B	GLN114
B	HOH425
B	HOH426

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11007792","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
A	TYR16	proton acceptor, proton donor
A	ASP40	proton acceptor, proton donor
A	ASP100	electrostatic stabiliser
A	ASP103	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
B	TYR16	proton acceptor, proton donor
B	ASP40	proton acceptor, proton donor
B	ASP100	electrostatic stabiliser
B	ASP103	electrostatic stabiliser

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