Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1J2T

Creatininase Mn

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	5
Details	BINDING SITE FOR RESIDUE ZN A 302

Chain	Residue
A	HIS36
A	ASP45
A	GLU183
A	MN301
A	HOH7008

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 301

Chain	Residue
A	HOH7008
A	HOH7009
A	GLU34
A	ASP45
A	HIS120
A	ZN302

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 302

Chain	Residue
B	HIS36
B	ASP45
B	GLU183
B	MN301
B	HOH7009

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

Chain	Residue
B	GLU34
B	ASP45
B	HIS120
B	ZN302
B	HOH7009
B	HOH7010

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 302

Chain	Residue
C	HIS36
C	ASP45
C	GLU183
C	MN301
C	HOH7010

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

Chain	Residue
C	GLU34
C	ASP45
C	HIS120
C	ZN302
C	HOH7010
C	HOH7011

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 302

Chain	Residue
D	HIS36
D	ASP45
D	GLU183
D	MN301
D	HOH7002

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN D 301

Chain	Residue
D	GLU34
D	ASP45
D	HIS120
D	ZN302
D	HOH7002
D	HOH7003

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 302

Chain	Residue
E	HIS36
E	ASP45
E	GLU183
E	MN301
E	HOH7004

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

Chain	Residue
E	GLU34
E	ASP45
E	HIS120
E	ZN302
E	HOH7004
E	HOH7005

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN F 302

Chain	Residue
F	HIS36
F	ASP45
F	GLU183
F	MN301
F	HOH7011

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

Chain	Residue
F	GLU34
F	ASP45
F	HIS120
F	ZN302
F	HOH7011
F	HOH7012

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 7001

Chain	Residue
D	LYS54
D	ARG55
D	TYR191
D	HOH7063
D	HOH7144
D	HOH7153

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 7002

Chain	Residue
B	LYS54
B	ARG55
B	TYR191
B	HOH7088
B	HOH7150
B	HOH7210

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 7003

Chain	Residue
E	LYS54
E	ARG55
E	TYR191
E	HOH7065
E	HOH7151
E	HOH7194

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 7004

Chain	Residue
F	LYS54
F	ARG55
F	TYR191
F	HOH7040
F	HOH7143
F	HOH7157

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 7005

Chain	Residue
C	LYS54
C	ARG55
C	TYR191
C	HOH7060
C	HOH7124
C	HOH7180

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 7006

Chain	Residue
A	HOH7057
A	HOH7131
A	HOH7262
A	LYS54
A	ARG55
A	TYR191

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 7007

Chain	Residue
A	ARG113
A	LYS147
A	GLU256
A	PHE257
A	HOH7118
A	HOH7245

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 7008

Chain	Residue
B	ARG113
B	LYS147
B	GLU256
B	PHE257
B	HOH7075
B	HOH7144
B	HOH7169

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 7009

Chain	Residue
C	ARG113
C	LYS147
C	GLU256
C	PHE257
C	HOH7075
C	HOH7220

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 7010

Chain	Residue
F	ARG113
F	LYS147
F	GLU256
F	PHE257
F	HOH7083

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:12946365, ECO:0000269\|PubMed:20043918, ECO:0007744\|PDB:3A6L

Chain	Residue	Details
A	GLU34
E	HIS120
F	GLU34
F	HIS120
A	HIS120
B	GLU34
B	HIS120
C	GLU34
C	HIS120
D	GLU34
D	HIS120
E	GLU34

site_id	SWS_FT_FI2
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269\|PubMed:12946365, ECO:0000269\|PubMed:15003455, ECO:0000269\|PubMed:20043918, ECO:0007744\|PDB:1V7Z, ECO:0007744\|PDB:3A6J, ECO:0007744\|PDB:3A6K, ECO:0007744\|PDB:3A6L

Chain	Residue	Details
A	HIS36
D	HIS36
D	ASP45
D	GLU183
E	HIS36
E	ASP45
E	GLU183
F	HIS36
F	ASP45
F	GLU183
A	ASP45
A	GLU183
B	HIS36
B	ASP45
B	GLU183
C	HIS36
C	ASP45
C	GLU183

site_id	SWS_FT_FI3
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:15003455, ECO:0000269\|PubMed:20043918, ECO:0007744\|PDB:1V7Z, ECO:0007744\|PDB:3A6J

Chain	Residue	Details
A	SER78
B	HIS178
C	SER78
C	TYR121
C	TRP174
C	ASP175
C	HIS178
D	SER78
D	TYR121
D	TRP174
D	ASP175
A	TYR121
D	HIS178
E	SER78
E	TYR121
E	TRP174
E	ASP175
E	HIS178
F	SER78
F	TYR121
F	TRP174
F	ASP175
A	TRP174
F	HIS178
A	ASP175
A	HIS178
B	SER78
B	TYR121
B	TRP174
B	ASP175

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Coordinates a catalytic water molecule

Chain	Residue	Details
A	GLU122
B	GLU122
C	GLU122
D	GLU122
E	GLU122
F	GLU122

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)