Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ZAB

Crystal Structure of Mouse Cytidine Deaminase Complexed with 3-Deazauridine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001882	molecular_function	nucleoside binding
A	0003824	molecular_function	catalytic activity
A	0004126	molecular_function	cytidine deaminase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006248	biological_process	CMP catabolic process
A	0006249	biological_process	dCMP catabolic process
A	0008270	molecular_function	zinc ion binding
A	0009972	biological_process	cytidine deamination
A	0016787	molecular_function	hydrolase activity
A	0019239	molecular_function	deaminase activity
A	0030308	biological_process	negative regulation of cell growth
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0044206	biological_process	UMP salvage
A	0045980	biological_process	negative regulation of nucleotide metabolic process
A	0046872	molecular_function	metal ion binding
A	0046898	biological_process	response to cycloheximide
A	0071217	biological_process	cellular response to external biotic stimulus
B	0001882	molecular_function	nucleoside binding
B	0003824	molecular_function	catalytic activity
B	0004126	molecular_function	cytidine deaminase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006248	biological_process	CMP catabolic process
B	0006249	biological_process	dCMP catabolic process
B	0008270	molecular_function	zinc ion binding
B	0009972	biological_process	cytidine deamination
B	0016787	molecular_function	hydrolase activity
B	0019239	molecular_function	deaminase activity
B	0030308	biological_process	negative regulation of cell growth
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0044206	biological_process	UMP salvage
B	0045980	biological_process	negative regulation of nucleotide metabolic process
B	0046872	molecular_function	metal ion binding
B	0046898	biological_process	response to cycloheximide
B	0071217	biological_process	cellular response to external biotic stimulus
C	0001882	molecular_function	nucleoside binding
C	0003824	molecular_function	catalytic activity
C	0004126	molecular_function	cytidine deaminase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006248	biological_process	CMP catabolic process
C	0006249	biological_process	dCMP catabolic process
C	0008270	molecular_function	zinc ion binding
C	0009972	biological_process	cytidine deamination
C	0016787	molecular_function	hydrolase activity
C	0019239	molecular_function	deaminase activity
C	0030308	biological_process	negative regulation of cell growth
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0044206	biological_process	UMP salvage
C	0045980	biological_process	negative regulation of nucleotide metabolic process
C	0046872	molecular_function	metal ion binding
C	0046898	biological_process	response to cycloheximide
C	0071217	biological_process	cellular response to external biotic stimulus
D	0001882	molecular_function	nucleoside binding
D	0003824	molecular_function	catalytic activity
D	0004126	molecular_function	cytidine deaminase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006248	biological_process	CMP catabolic process
D	0006249	biological_process	dCMP catabolic process
D	0008270	molecular_function	zinc ion binding
D	0009972	biological_process	cytidine deamination
D	0016787	molecular_function	hydrolase activity
D	0019239	molecular_function	deaminase activity
D	0030308	biological_process	negative regulation of cell growth
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0044206	biological_process	UMP salvage
D	0045980	biological_process	negative regulation of nucleotide metabolic process
D	0046872	molecular_function	metal ion binding
D	0046898	biological_process	response to cycloheximide
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	HOH1006

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

Chain	Residue
B	CYS65
B	CYS99
B	CYS102
B	HOH1003

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

Chain	Residue
C	CYS99
C	CYS102
C	HOH1004
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	HOH1005

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 1005

Chain	Residue
A	GLN130
A	GLN130
A	ALA135
A	ALA135
A	HOH1010
A	HOH1010
A	HOH1070
A	HOH1070

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE URD A 1001

Chain	Residue
A	PHE36
A	VAL38
A	ASN54
A	GLU56
A	CYS65
A	ALA66
A	GLU67
A	ILE96
A	SER97
A	PRO98
A	HOH1007
C	ALA58
C	CYS59
C	TYR60
C	PRO61

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE URD B 1002

Chain	Residue
A	PHE137
B	PHE36
B	VAL38
B	ASN54
B	GLU56
B	CYS65
B	ALA66
B	GLU67
B	SER97
B	HOH1003
B	HOH1004
D	ALA58
D	CYS59
D	TYR60
D	PRO61

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE URD C 1003

Chain	Residue
A	ALA58
A	CYS59
A	TYR60
A	PRO61
C	PHE36
C	VAL38
C	ASN54
C	GLU56
C	VAL64
C	CYS65
C	ALA66
C	GLU67
C	SER97
C	PRO98
C	HOH1005

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE URD D 1004

Chain	Residue
B	ALA58
B	CYS59
B	TYR60
B	PRO61
D	PHE36
D	VAL38
D	ASN54
D	GLU56
D	CYS65
D	ALA66
D	GLU67
D	SER97
D	PRO98
D	HOH1005
D	HOH1006

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	4
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:16784234

Chain	Residue	Details
A	GLU67
B	GLU67
C	GLU67
D	GLU67

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING:

Chain	Residue	Details
A	ASN54
C	CYS65
C	CYS99
C	CYS102
D	ASN54
D	CYS65
D	CYS99
D	CYS102
A	CYS65
A	CYS99
A	CYS102
B	ASN54
B	CYS65
B	CYS99
B	CYS102
C	ASN54

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)