5G2G

Crystal structure of ketosteroid isomerase containing M116K mutation in the equilenin-bound form

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	11
Details	BINDING SITE FOR RESIDUE EQU A 1129

Chain	Residue
A	TYR16
A	HOH2030
B	ASN93
A	ASP40
A	PHE86
A	MET90
A	LEU99
A	ASP103
A	LYS116
A	TRP120
A	HOH2029

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EQU B 1129

Chain	Residue
B	TYR16
B	ASP40
B	VAL88
B	LEU99
B	ASP103
B	LYS116
B	TRP120

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	TYR16
B	TYR16

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP40
B	ASP40

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11007792

Chain	Residue	Details
A	ASP103
B	ASP103

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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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