Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2FR5

Crystal Structure of Mouse Cytidine Deaminase Complexed with Tetrahydrouridine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001882	molecular_function	nucleoside binding
A	0004126	molecular_function	cytidine deaminase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006217	biological_process	deoxycytidine catabolic process
A	0006248	biological_process	CMP catabolic process
A	0006249	biological_process	dCMP catabolic process
A	0008270	molecular_function	zinc ion binding
A	0009173	biological_process	pyrimidine ribonucleoside monophosphate metabolic process
A	0009218	biological_process	pyrimidine ribonucleotide metabolic process
A	0016787	molecular_function	hydrolase activity
A	0019239	molecular_function	deaminase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0044206	biological_process	UMP salvage
A	0046109	biological_process	uridine biosynthetic process
A	0071217	biological_process	cellular response to external biotic stimulus
B	0001882	molecular_function	nucleoside binding
B	0004126	molecular_function	cytidine deaminase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006217	biological_process	deoxycytidine catabolic process
B	0006248	biological_process	CMP catabolic process
B	0006249	biological_process	dCMP catabolic process
B	0008270	molecular_function	zinc ion binding
B	0009173	biological_process	pyrimidine ribonucleoside monophosphate metabolic process
B	0009218	biological_process	pyrimidine ribonucleotide metabolic process
B	0016787	molecular_function	hydrolase activity
B	0019239	molecular_function	deaminase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0044206	biological_process	UMP salvage
B	0046109	biological_process	uridine biosynthetic process
B	0071217	biological_process	cellular response to external biotic stimulus
C	0001882	molecular_function	nucleoside binding
C	0004126	molecular_function	cytidine deaminase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006217	biological_process	deoxycytidine catabolic process
C	0006248	biological_process	CMP catabolic process
C	0006249	biological_process	dCMP catabolic process
C	0008270	molecular_function	zinc ion binding
C	0009173	biological_process	pyrimidine ribonucleoside monophosphate metabolic process
C	0009218	biological_process	pyrimidine ribonucleotide metabolic process
C	0016787	molecular_function	hydrolase activity
C	0019239	molecular_function	deaminase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0044206	biological_process	UMP salvage
C	0046109	biological_process	uridine biosynthetic process
C	0071217	biological_process	cellular response to external biotic stimulus
D	0001882	molecular_function	nucleoside binding
D	0004126	molecular_function	cytidine deaminase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006217	biological_process	deoxycytidine catabolic process
D	0006248	biological_process	CMP catabolic process
D	0006249	biological_process	dCMP catabolic process
D	0008270	molecular_function	zinc ion binding
D	0009173	biological_process	pyrimidine ribonucleoside monophosphate metabolic process
D	0009218	biological_process	pyrimidine ribonucleotide metabolic process
D	0016787	molecular_function	hydrolase activity
D	0019239	molecular_function	deaminase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0044206	biological_process	UMP salvage
D	0046109	biological_process	uridine biosynthetic process
D	0071217	biological_process	cellular response to external biotic stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 147

Chain	Residue
A	CYS65
A	CYS99
A	CYS102
A	TYU1001

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 147

Chain	Residue
B	CYS65
B	CYS99
B	CYS102
B	TYU1002

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 147

Chain	Residue
C	CYS99
C	CYS102
C	TYU1003
C	CYS65

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 147

Chain	Residue
D	CYS65
D	CYS99
D	CYS102
D	TYU1004

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 1005

Chain	Residue
A	GLN130
A	GLN130
A	PRO134
A	ALA135
A	ALA135
A	SER136
A	HOH1008
A	HOH1008
A	HOH1065
A	HOH1065

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE TYU A 1001

Chain	Residue
A	PHE36
A	VAL38
A	ASN54
A	GLU56
A	CYS65
A	ALA66
A	GLU67
A	CYS99
A	CYS102
A	ZN147
A	HOH1031
B	PHE137
C	ALA58
C	CYS59
C	TYR60
C	PRO61

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE TYU B 1002

Chain	Residue
A	PHE137
B	PHE36
B	VAL38
B	ASN54
B	GLU56
B	CYS65
B	ALA66
B	GLU67
B	PRO98
B	CYS99
B	CYS102
B	ZN147
B	HOH1016
D	ALA58
D	CYS59
D	TYR60
D	PRO61

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE TYU C 1003

Chain	Residue
A	ALA58
A	CYS59
A	TYR60
A	PRO61
C	PHE36
C	VAL38
C	ASN54
C	GLU56
C	CYS65
C	ALA66
C	GLU67
C	CYS99
C	CYS102
C	ZN147
C	HOH1024
D	PHE137

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE TYU D 1004

Chain	Residue
B	ALA58
B	CYS59
B	TYR60
B	PRO61
C	PHE137
D	PHE36
D	VAL38
D	ASN54
D	GLU56
D	CYS65
D	ALA66
D	GLU67
D	PRO98
D	CYS99
D	CYS102
D	ZN147
D	HOH1065

Functional Information from PROSITE/UniProt

site_id	PS00903
Number of Residues	42
Details	CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. CAErtAIqkaisegykdfraiaissdlqeefis.......PCga......CrqvM

Chain	Residue	Details
A	CYS65-MET106

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	508
Details	Domain: {"description":"CMP/dCMP-type deaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"16784234","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU67

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

Chain	Residue	Details
B	GLU67

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

Chain	Residue	Details
C	GLU67

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

Chain	Residue	Details
D	GLU67

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)