Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3A6J

E122Q mutant creatininase complexed with creatine

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	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS36
A	ASP45
A	GLU183
A	CRN303

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CRN A 303

Chain	Residue
A	TYR121
A	TRP174
A	ASP175
A	HIS178
A	GLU183
A	ZN301
A	GLU34
A	HIS36
A	ASP45
A	SER78
A	HIS120

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 403

Chain	Residue
A	ARG113
A	LYS147
A	GLU256
A	PHE257
A	HOH1230
A	HOH1452
A	HOH1651

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 409

Chain	Residue
A	LYS54
A	ARG55
A	TYR191
A	HOH1137

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 415

Chain	Residue
A	ARG59
A	GLN247
A	ARG254

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS36
B	ASP45
B	GLU183
B	CRN304

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CRN B 304

Chain	Residue
B	GLU34
B	HIS36
B	ASP45
B	SER78
B	HIS120
B	TYR121
B	TRP174
B	ASP175
B	GLU177
B	HIS178
B	GLU183
B	ZN301
B	HOH1124

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 410

Chain	Residue
B	LYS54
B	ARG55
B	TYR191
B	HOH1128

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 416

Chain	Residue
B	ARG59
B	GLN247
B	ARG254

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS36
C	ASP45
C	GLU183
C	CRN305

site_id	BC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CRN C 305

Chain	Residue
C	GLU34
C	HIS36
C	ASP45
C	SER78
C	HIS120
C	TYR121
C	TRP174
C	ASP175
C	GLU177
C	HIS178
C	GLU183
C	ZN301

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 411

Chain	Residue
C	LYS54
C	ARG55
C	TYR191
C	HOH1177

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 417

Chain	Residue
C	ARG59
C	GLN247
C	ARG254

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

Chain	Residue
D	HIS36
D	ASP45
D	GLU183
D	HOH1001

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 400

Chain	Residue
D	ARG59
D	GLN247
D	ARG254

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 412

Chain	Residue
D	LYS54
D	ARG55
D	TYR191
D	HOH1164
D	HOH1717

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

Chain	Residue
E	HIS36
E	ASP45
E	GLU183
E	CRN306

site_id	BC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CRN E 306

Chain	Residue
E	TRP174
E	ASP175
E	HIS178
E	GLU183
E	ZN301
E	GLU34
E	HIS36
E	ASP45
E	SER78
E	HIS120
E	TYR121
E	TRP154

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 401

Chain	Residue
E	ARG59
E	GLN247
E	ARG254

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 413

Chain	Residue
E	LYS54
E	ARG55
E	TYR191
E	HOH1376

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 301

Chain	Residue
F	HIS36
F	ASP45
F	GLU183
F	CRN307

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CRN F 307

Chain	Residue
F	GLU34
F	HIS36
F	ASP45
F	SER78
F	HIS120
F	TYR121
F	TRP174
F	ASP175
F	GLU177
F	HIS178
F	GLU183
F	ZN301

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F 402

Chain	Residue
F	ARG59
F	GLN247
F	ARG254

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 414

Chain	Residue
F	LYS54
F	ARG55
F	TYR191
F	HOH1213
F	HOH1540

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	GLN122	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	GLN122	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	GLN122	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	GLN122	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	GLN122	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	GLN122	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)