Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3A6E

W174F mutant creatininase, type I

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 MN A 300

Chain	Residue
A	GLU34
A	ASP45
A	HIS120
A	CAC302
A	HOH1082

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS36
A	ASP45
A	GLU183
A	CAC302

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CAC A 302

Chain	Residue
A	GLU34
A	HIS36
A	ASP45
A	SER78
A	GLY119
A	HIS120
A	TYR121
A	TRP154
A	HIS178
A	GLU183
A	MN300
A	ZN301
A	HOH1082

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 300

Chain	Residue
B	GLU34
B	ASP45
B	HIS120
B	ZN301
B	CAC303
B	HOH1135

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS36
B	ASP45
B	GLU183
B	MN300
B	CAC303

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CAC B 303

Chain	Residue
B	GLU34
B	HIS36
B	ASP45
B	SER78
B	GLY119
B	HIS120
B	TYR121
B	TRP154
B	HIS178
B	GLU183
B	MN300
B	ZN301
B	HOH1135

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 300

Chain	Residue
C	GLU34
C	ASP45
C	HIS120
C	CAC304
C	HOH1177

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS36
C	ASP45
C	GLU183
C	CAC304

site_id	AC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CAC C 304

Chain	Residue
C	GLU34
C	HIS36
C	ASP45
C	SER78
C	GLY119
C	HIS120
C	TYR121
C	TRP154
C	HIS178
C	GLU183
C	MN300
C	ZN301
C	HOH1177

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN D 300

Chain	Residue
D	GLU34
D	ASP45
D	HIS120
D	ZN301
D	CAC305
D	HOH1074

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS36
D	ASP45
D	GLU183
D	MN300
D	CAC305

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CAC D 305

Chain	Residue
D	GLU34
D	HIS36
D	ASP45
D	SER78
D	GLY119
D	HIS120
D	TYR121
D	TRP154
D	HIS178
D	GLU183
D	MN300
D	ZN301
D	HOH1074

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN E 300

Chain	Residue
E	GLU34
E	ASP45
E	HIS120
E	CAC306
E	HOH1289

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 301

Chain	Residue
E	GLU183
E	CAC306
E	HIS36
E	ASP45

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CAC E 306

Chain	Residue
E	HIS36
E	ASP45
E	SER78
E	GLY119
E	HIS120
E	TYR121
E	TRP154
E	HIS178
E	GLU183
E	MN300
E	ZN301
E	HOH1289

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 300

Chain	Residue
F	GLU34
F	ASP45
F	HIS120
F	CAC307
F	HOH1246

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 301

Chain	Residue
F	HIS36
F	ASP45
F	GLU183
F	CAC307

site_id	BC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CAC F 307

Chain	Residue
F	GLU34
F	HIS36
F	ASP45
F	SER78
F	GLY119
F	HIS120
F	TYR121
F	TRP154
F	HIS178
F	GLU183
F	MN300
F	ZN301
F	HOH1246

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	PHE174
C	ASP175
C	HIS178
D	SER78
D	TYR121
D	PHE174
D	ASP175
A	TYR121
D	HIS178
E	SER78
E	TYR121
E	PHE174
E	ASP175
E	HIS178
F	SER78
F	TYR121
F	PHE174
F	ASP175
A	PHE174
F	HIS178
A	ASP175
A	HIS178
B	SER78
B	TYR121
B	PHE174
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)
		EDMap 2fo-fc (MTZ)