Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Q3K

Crystal structure of creatinine amidohydrolase (creatininase)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006601	biological_process	creatine biosynthetic process
A	0006602	biological_process	creatinine catabolic process
A	0008270	molecular_function	zinc ion binding
A	0009231	biological_process	riboflavin biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
A	0047789	molecular_function	creatininase activity
B	0006601	biological_process	creatine biosynthetic process
B	0006602	biological_process	creatinine catabolic process
B	0008270	molecular_function	zinc ion binding
B	0009231	biological_process	riboflavin biosynthetic process
B	0016787	molecular_function	hydrolase activity
B	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
B	0047789	molecular_function	creatininase activity
C	0006601	biological_process	creatine biosynthetic process
C	0006602	biological_process	creatinine catabolic process
C	0008270	molecular_function	zinc ion binding
C	0009231	biological_process	riboflavin biosynthetic process
C	0016787	molecular_function	hydrolase activity
C	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
C	0047789	molecular_function	creatininase activity
D	0006601	biological_process	creatine biosynthetic process
D	0006602	biological_process	creatinine catabolic process
D	0008270	molecular_function	zinc ion binding
D	0009231	biological_process	riboflavin biosynthetic process
D	0016787	molecular_function	hydrolase activity
D	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
D	0047789	molecular_function	creatininase activity
E	0006601	biological_process	creatine biosynthetic process
E	0006602	biological_process	creatinine catabolic process
E	0008270	molecular_function	zinc ion binding
E	0009231	biological_process	riboflavin biosynthetic process
E	0016787	molecular_function	hydrolase activity
E	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
E	0047789	molecular_function	creatininase activity
F	0006601	biological_process	creatine biosynthetic process
F	0006602	biological_process	creatinine catabolic process
F	0008270	molecular_function	zinc ion binding
F	0009231	biological_process	riboflavin biosynthetic process
F	0016787	molecular_function	hydrolase activity
F	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding
F	0047789	molecular_function	creatininase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A 300

Chain	Residue
A	GLU34
A	ASP45
A	HIS120
A	ZN301
A	HOH903
A	HOH904
A	HOH905

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	GLU183
A	ZN300
A	HOH903
A	HIS36
A	ASP45

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN B 300

Chain	Residue
B	GLU34
B	ASP45
B	HIS120
B	ZN301
B	HOH902
B	HOH903
B	HOH904

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS36
B	ASP45
B	GLU183
B	ZN300
B	HOH902
B	HOH905

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN C 300

Chain	Residue
C	GLU34
C	ASP45
C	HIS120
C	ZN301
C	HOH905
C	HOH906
C	HOH907

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS36
C	ASP45
C	GLU183
C	ZN300
C	HOH905
C	HOH908

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN D 300

Chain	Residue
D	GLU34
D	ASP45
D	HIS120
D	ZN301
D	HOH302
D	HOH303

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS36
D	ASP45
D	GLU183
D	ZN300
D	HOH302

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN E 300

Chain	Residue
E	GLU34
E	ASP45
E	HIS120
E	ZN301
E	HOH905
E	HOH907

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN E 301

Chain	Residue
E	HIS36
E	ASP45
E	GLU183
E	ZN300
E	HOH904
E	HOH906

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN F 300

Chain	Residue
F	GLU34
F	ASP45
F	HIS120
F	ZN301
F	HOH302
F	HOH303

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN F 301

Chain	Residue
F	HIS36
F	ASP45
F	GLU183
F	ZN300
F	HOH302
F	HOH304

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 901

Chain	Residue
B	VAL19
B	GLY22
B	ASP23
B	CYS24
B	GLY110
B	ARG112
B	ARG113

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 902

Chain	Residue
A	LEU68
A	GLN69
A	TYR70
B	GLN69
B	TYR70
B	THR98
B	HOH982

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 903

Chain	Residue
E	LEU68
E	GLN69
E	TYR70
E	HOH911
E	HOH1005
F	LEU68
F	GLN69
F	TYR70

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 904

Chain	Residue
D	GLN69
D	TYR70
D	THR98
C	LEU68
C	GLN69
C	TYR70
C	HOH913

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12946365","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20043918","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3A6L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12946365","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15003455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20043918","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1V7Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A6J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A6K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A6L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15003455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20043918","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1V7Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A6J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Site: {"description":"Coordinates a catalytic water molecule"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 720

Chain	Residue	Details
A	GLU34	metal ligand
A	HIS36	metal ligand
A	ASP45	metal ligand
A	HIS120	metal ligand
A	GLU122	electrostatic stabiliser
A	HIS178	proton acceptor, proton donor
A	GLU183	metal ligand

site_id	MCSA2
Number of Residues	7
Details	M-CSA 720

Chain	Residue	Details
B	GLU34	metal ligand
B	HIS36	metal ligand
B	ASP45	metal ligand
B	HIS120	metal ligand
B	GLU122	electrostatic stabiliser
B	HIS178	proton acceptor, proton donor
B	GLU183	metal ligand

site_id	MCSA3
Number of Residues	7
Details	M-CSA 720

Chain	Residue	Details
C	GLU34	metal ligand
C	HIS36	metal ligand
C	ASP45	metal ligand
C	HIS120	metal ligand
C	GLU122	electrostatic stabiliser
C	HIS178	proton acceptor, proton donor
C	GLU183	metal ligand

site_id	MCSA4
Number of Residues	7
Details	M-CSA 720

Chain	Residue	Details
D	GLU34	metal ligand
D	HIS36	metal ligand
D	ASP45	metal ligand
D	HIS120	metal ligand
D	GLU122	electrostatic stabiliser
D	HIS178	proton acceptor, proton donor
D	GLU183	metal ligand

site_id	MCSA5
Number of Residues	7
Details	M-CSA 720

Chain	Residue	Details
E	GLU34	metal ligand
E	HIS36	metal ligand
E	ASP45	metal ligand
E	HIS120	metal ligand
E	GLU122	electrostatic stabiliser
E	HIS178	proton acceptor, proton donor
E	GLU183	metal ligand

site_id	MCSA6
Number of Residues	7
Details	M-CSA 720

Chain	Residue	Details
F	GLU34	metal ligand
F	HIS36	metal ligand
F	ASP45	metal ligand
F	HIS120	metal ligand
F	GLU122	electrostatic stabiliser
F	HIS178	proton acceptor, proton donor
F	GLU183	metal ligand

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