1RAK

Bacterial cytosine deaminase D314S mutant bound to 5-fluoro-4-(S)-hydroxyl-3,4-dihydropyrimidine.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004131	molecular_function	cytosine deaminase activity
A	0005829	cellular_component	cytosol
A	0006209	biological_process	cytosine catabolic process
A	0008198	molecular_function	ferrous iron binding
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0016814	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
A	0019239	molecular_function	deaminase activity
A	0019858	biological_process	cytosine metabolic process
A	0035888	molecular_function	isoguanine deaminase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 500

Chain	Residue
A	HIS61
A	HIS63
A	HIS214
A	ASP313
A	FPY501

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FPY A 501

Chain	Residue
A	GLN156
A	ILE183
A	HIS214
A	GLU217
A	HIS246
A	ASP313
A	SER314
A	TRP319
A	FE500
A	HOH665
A	HIS61
A	HIS63
A	LEU81
A	PHE154

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 502

Chain	Residue
A	ALA128
A	LYS134
A	ARG174
A	LEU175
A	HOH951
A	HOH951
A	HOH976

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11812140","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of cytosine deaminase from Escherichia coli complexed with two zinc atoms in the active site.","authors":["Fedorov A.A.","Fedorov E.V.","Kamat S.","Hitchcock D.","Raushel F.M.","Almo S.C."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11812140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15381761","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11812140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15381761","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Activates the nucleophilic water","evidences":[{"source":"PubMed","id":"21545144","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21604715","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 710

Chain	Residue	Details
A	HIS61	metal ligand
A	HIS63	metal ligand
A	GLN156	electrostatic stabiliser
A	HIS214	metal ligand
A	GLU217	proton acceptor, proton donor
A	ASP313	metal ligand

---