6U1Z

Crystal Structure of Ketosteroid Isomerase from Pseudomonas Putida (pKSI) at 280 K

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	6
Details	binding site for residue MG B 201

Chain	Residue
B	HOH308
B	HOH324
B	HOH373
B	HOH384
B	HOH385
B	HOH389

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CL B 202

Chain	Residue
B	HOH378
A	THR71
B	GLY72
B	ARG75

---

site_id	AC3
Number of Residues	5
Details	binding site for residue CL A 201

Chain	Residue
A	GLY72
A	ARG75
B	THR71
B	HOH355
B	HOH378

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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

---

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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