3A6K
The E122Q mutant creatininase, Mn-Zn type
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 | ZN301 |
A | CL302 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | CL302 |
A | HIS36 |
A | ASP45 |
A | GLU183 |
A | MN300 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 302 |
Chain | Residue |
A | MN300 |
A | ZN301 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 300 |
Chain | Residue |
B | GLU34 |
B | ASP45 |
B | HIS120 |
B | ZN301 |
B | CL302 |
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 | CL302 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 302 |
Chain | Residue |
B | HIS178 |
B | GLU183 |
B | MN300 |
B | ZN301 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 300 |
Chain | Residue |
C | GLU34 |
C | ASP45 |
C | HIS120 |
C | ZN301 |
C | CL302 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 301 |
Chain | Residue |
C | HIS36 |
C | ASP45 |
C | GLU183 |
C | MN300 |
C | CL302 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 302 |
Chain | Residue |
C | HIS178 |
C | MN300 |
C | ZN301 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN D 300 |
Chain | Residue |
D | GLU34 |
D | ASP45 |
D | HIS120 |
D | CL302 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 301 |
Chain | Residue |
D | HIS36 |
D | ASP45 |
D | GLU183 |
D | CL302 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL D 302 |
Chain | Residue |
D | MN300 |
D | ZN301 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN E 300 |
Chain | Residue |
E | GLU34 |
E | ASP45 |
E | HIS120 |
E | ZN301 |
E | CL302 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 301 |
Chain | Residue |
E | HIS36 |
E | ASP45 |
E | GLU183 |
E | MN300 |
E | CL302 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL E 302 |
Chain | Residue |
E | MN300 |
E | ZN301 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN F 300 |
Chain | Residue |
F | GLU34 |
F | ASP45 |
F | HIS120 |
F | ZN301 |
F | CL302 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 301 |
Chain | Residue |
F | HIS36 |
F | ASP45 |
F | GLU183 |
F | MN300 |
F | CL302 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL F 302 |
Chain | Residue |
F | MN300 |
F | ZN301 |
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 | GLN122 | |
B | GLN122 | |
C | GLN122 | |
D | GLN122 | |
E | GLN122 | |
F | GLN122 |
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 |