3A6G
W154F mutant 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 MN A 300 |
| Chain | Residue |
| A | GLU34 |
| A | ASP45 |
| A | HIS120 |
| A | ZN301 |
| A | HOH1001 |
| A | HOH1002 |
| A | HOH1515 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | GLU183 |
| A | MN300 |
| A | HOH1001 |
| A | HIS36 |
| A | ASP45 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN B 300 |
| Chain | Residue |
| B | GLU34 |
| B | ASP45 |
| B | HIS120 |
| B | ZN301 |
| B | HOH1003 |
| B | HOH1004 |
| B | HOH1013 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HIS36 |
| B | ASP45 |
| B | GLU183 |
| B | MN300 |
| B | HOH1003 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN C 300 |
| Chain | Residue |
| C | GLU34 |
| C | ASP45 |
| C | HIS120 |
| C | ZN301 |
| C | HOH1005 |
| C | HOH1006 |
| C | HOH1014 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 301 |
| Chain | Residue |
| C | HIS36 |
| C | ASP45 |
| C | GLU183 |
| C | MN300 |
| C | HOH1005 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN D 300 |
| Chain | Residue |
| D | GLU34 |
| D | ASP45 |
| D | HIS120 |
| D | ZN301 |
| D | HOH1007 |
| D | HOH1008 |
| D | HOH1015 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | HIS36 |
| D | ASP45 |
| D | GLU183 |
| D | MN300 |
| D | HOH1007 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN E 300 |
| Chain | Residue |
| E | GLU34 |
| E | ASP45 |
| E | HIS120 |
| E | ZN301 |
| E | HOH1009 |
| E | HOH1010 |
| E | HOH1016 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 301 |
| Chain | Residue |
| E | HIS36 |
| E | ASP45 |
| E | GLU183 |
| E | MN300 |
| E | HOH1009 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN F 300 |
| Chain | Residue |
| F | GLU34 |
| F | ASP45 |
| F | HIS120 |
| F | ZN301 |
| F | HOH1011 |
| F | HOH1012 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN F 301 |
| Chain | Residue |
| F | HIS36 |
| F | ASP45 |
| F | GLU183 |
| F | MN300 |
| F | HOH1011 |
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 | 29 |
| 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 |
