5KP1

Crystal Structure of Ketosteroid Isomerase from Pseudomonas putida (pKSI) bound to Equilenin; D40N, Y16(Cl-Y)

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
C	0004769	molecular_function	steroid Delta-isomerase activity
C	0006629	biological_process	lipid metabolic process
C	0008202	biological_process	steroid metabolic process
C	0016853	molecular_function	isomerase activity
D	0004769	molecular_function	steroid Delta-isomerase activity
D	0006629	biological_process	lipid metabolic process
D	0008202	biological_process	steroid metabolic process
D	0016853	molecular_function	isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue EQU A 201

Chain	Residue
A	3CT16
C	TRP92
C	ASN93
A	ASN40
A	VAL88
A	MET90
A	LEU99
A	ASP103
A	MET116
A	TRP120
A	HOH315

---

site_id	AC2
Number of Residues	8
Details	binding site for residue SO4 A 202

Chain	Residue
A	THR5
A	ALA6
A	HIS78
A	HOH302
A	HOH314
A	HOH322
A	HOH404
A	HOH410

---

site_id	AC3
Number of Residues	9
Details	binding site for residue EQU B 200

Chain	Residue
B	3CT16
B	ASN40
B	MET90
B	LEU99
B	ASP103
B	MET116
B	TRP120
B	HOH312
D	ASN93

---

site_id	AC4
Number of Residues	11
Details	binding site for residue EQU C 200

Chain	Residue
A	TRP92
A	ASN93
C	3CT16
C	ASN40
C	PHE86
C	MET90
C	LEU99
C	ASP103
C	MET116
C	TRP120
C	HOH314

---

site_id	AC5
Number of Residues	11
Details	binding site for residue EQU D 201

Chain	Residue
B	TRP92
B	ASN93
D	3CT16
D	ASN40
D	VAL88
D	MET90
D	LEU99
D	ASP103
D	MET116
D	TRP120
D	HOH358

---

site_id	AC6
Number of Residues	7
Details	binding site for residue SO4 D 202

Chain	Residue
D	THR5
D	ALA6
D	HIS78
D	HOH310
D	HOH312
D	HOH403
D	HOH410

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	3CT16
B	3CT16
C	3CT16
D	3CT16

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASN40
B	ASN40
C	ASN40
D	ASN40

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11007792

Chain	Residue	Details
A	ASP103
B	ASP103
C	ASP103
D	ASP103

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
A	3CT16	proton acceptor, proton donor
A	GLN44	proton acceptor, proton donor
A	VAL104	electrostatic stabiliser
A	PHE107	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
B	3CT16	proton acceptor, proton donor
B	GLN44	proton acceptor, proton donor
B	VAL104	electrostatic stabiliser
B	PHE107	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
C	3CT16	proton acceptor, proton donor
C	GLN44	proton acceptor, proton donor
C	VAL104	electrostatic stabiliser
C	PHE107	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
D	3CT16	proton acceptor, proton donor
D	GLN44	proton acceptor, proton donor
D	VAL104	electrostatic stabiliser
D	PHE107	electrostatic stabiliser

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