2PZV

Crystal Structure of Ketosteroid Isomerase D40N from Pseudomonas Putida (pksi) with bound Phenol

Replaces:  2B32

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	5
Details	BINDING SITE FOR RESIDUE IPH A 401

Chain	Residue
A	TYR16
A	ASN40
A	PHE86
A	ASP103
A	MET116

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPH B 402

Chain	Residue
B	MET116
B	TYR16
B	ASN40
B	PHE86
B	ASP103

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPH C 403

Chain	Residue
C	TYR16
C	ASN40
C	PHE86
C	ASP103
C	MET116

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPH D 404

Chain	Residue
D	TYR16
D	ASN40
D	PHE86
D	ASP103
D	MET116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11007792","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1e3v

Chain	Residue	Details
A	ASP103
A	ASN40
A	TYR32
A	TYR16
A	TYR57

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1e3v

Chain	Residue	Details
B	ASP103
B	ASN40
B	TYR32
B	TYR16
B	TYR57

---

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1e3v

Chain	Residue	Details
C	ASP103
C	ASN40
C	TYR32
C	TYR16
C	TYR57

---

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1e3v

Chain	Residue	Details
D	ASP103
D	ASN40
D	TYR32
D	TYR16
D	TYR57

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
A	TYR16	proton acceptor, proton donor
A	ASN40	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	ASN40	proton acceptor, proton donor
B	ASP100	electrostatic stabiliser
B	ASP103	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
C	TYR16	proton acceptor, proton donor
C	ASN40	proton acceptor, proton donor
C	ASP100	electrostatic stabiliser
C	ASP103	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	4
Details	M-CSA 349

Chain	Residue	Details
D	TYR16	proton acceptor, proton donor
D	ASN40	proton acceptor, proton donor
D	ASP100	electrostatic stabiliser
D	ASP103	electrostatic stabiliser

---