1V7Z
creatininase-product complex
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 | 6 |
Details | BINDING SITE FOR RESIDUE MN A 300 |
Chain | Residue |
A | GLU34 |
A | ASP45 |
A | HIS120 |
A | ZN301 |
A | CRN401 |
A | HOH1001 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | MN300 |
A | CRN401 |
A | HIS36 |
A | ASP45 |
A | GLU183 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 3300 |
Chain | Residue |
B | GLU34 |
B | ASP45 |
B | HIS120 |
B | HOH1003 |
B | ZN3301 |
B | CRN3401 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 3301 |
Chain | Residue |
B | HIS36 |
B | ASP45 |
B | GLU183 |
B | MN3300 |
B | CRN3401 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 4300 |
Chain | Residue |
C | GLU34 |
C | ASP45 |
C | HIS120 |
C | HOH1005 |
C | ZN4301 |
C | CRN4401 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 4301 |
Chain | Residue |
C | HIS36 |
C | ASP45 |
C | GLU183 |
C | MN4300 |
C | CRN4401 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 5300 |
Chain | Residue |
D | GLU34 |
D | ASP45 |
D | HIS120 |
D | HOH1007 |
D | ZN5301 |
D | CRN5401 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 5301 |
Chain | Residue |
D | HIS36 |
D | ASP45 |
D | GLU183 |
D | MN5300 |
D | CRN5401 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 6300 |
Chain | Residue |
E | GLU34 |
E | ASP45 |
E | HIS120 |
E | HOH1009 |
E | ZN6301 |
E | CRN6401 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 6301 |
Chain | Residue |
E | HIS36 |
E | ASP45 |
E | GLU183 |
E | MN6300 |
E | CRN6401 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 7300 |
Chain | Residue |
F | GLU34 |
F | ASP45 |
F | HIS120 |
F | HOH1011 |
F | ZN7301 |
F | CRN7401 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 7301 |
Chain | Residue |
F | HIS36 |
F | ASP45 |
F | GLU183 |
F | MN7300 |
F | CRN7401 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | LYS54 |
A | ARG55 |
A | TYR191 |
A | HOH1158 |
A | HOH1732 |
A | HOH2649 |
A | HOH2699 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | ARG59 |
A | GLN247 |
A | ARG254 |
A | HOH2407 |
A | HOH2754 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | ARG113 |
A | LYS147 |
A | GLU256 |
A | PHE257 |
A | HOH1819 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 3501 |
Chain | Residue |
B | LYS54 |
B | ARG55 |
B | TYR191 |
B | HOH1136 |
B | HOH1841 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 3502 |
Chain | Residue |
B | ARG59 |
B | GLN247 |
B | ARG254 |
B | HOH2247 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 3503 |
Chain | Residue |
B | ARG113 |
B | LYS147 |
B | GLU256 |
B | PHE257 |
B | HOH1592 |
B | HOH2365 |
B | HOH2378 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 4501 |
Chain | Residue |
C | LYS54 |
C | ARG55 |
C | TYR191 |
C | HOH1166 |
C | HOH1959 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 4502 |
Chain | Residue |
C | ARG59 |
C | GLN247 |
C | ARG254 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 C 4503 |
Chain | Residue |
C | ARG113 |
C | LYS147 |
C | GLU256 |
C | PHE257 |
C | PRO258 |
C | HOH1480 |
C | HOH2715 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 5501 |
Chain | Residue |
D | LYS54 |
D | ARG55 |
D | TYR191 |
D | HOH1398 |
D | HOH2278 |
D | HOH2558 |
site_id | CC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 5502 |
Chain | Residue |
D | ARG59 |
D | GLN247 |
D | ARG254 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 5503 |
Chain | Residue |
D | ARG113 |
D | LYS147 |
D | GLU256 |
D | PHE257 |
D | HOH1736 |
D | HOH2369 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 6501 |
Chain | Residue |
E | LYS54 |
E | ARG55 |
E | TYR191 |
E | HOH1375 |
E | HOH2743 |
site_id | CC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 6502 |
Chain | Residue |
E | ARG59 |
E | GLN247 |
E | ARG254 |
site_id | CC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 6503 |
Chain | Residue |
E | ARG113 |
E | LYS147 |
E | GLU256 |
E | PHE257 |
E | HOH1424 |
site_id | DC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 F 7501 |
Chain | Residue |
F | LYS54 |
F | ARG55 |
F | TYR191 |
F | HOH1174 |
F | HOH1903 |
F | HOH2400 |
site_id | DC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 F 7502 |
Chain | Residue |
F | ARG59 |
F | GLN247 |
F | ARG254 |
site_id | DC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 F 7503 |
Chain | Residue |
F | ARG113 |
F | LYS147 |
F | GLU256 |
F | PHE257 |
F | HOH1579 |
F | HOH1979 |
F | HOH2493 |
site_id | DC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CRN A 401 |
Chain | Residue |
A | GLU34 |
A | HIS36 |
A | ASP45 |
A | SER78 |
A | GLY119 |
A | HIS120 |
A | TYR121 |
A | TRP174 |
A | ASP175 |
A | GLU177 |
A | HIS178 |
A | GLU183 |
A | MN300 |
A | ZN301 |
A | HOH1001 |
site_id | DC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CRN B 3401 |
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 | HOH1003 |
B | HOH2653 |
B | MN3300 |
B | ZN3301 |
site_id | DC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CRN C 4401 |
Chain | Residue |
C | GLU34 |
C | HIS36 |
C | ASP45 |
C | SER78 |
C | GLY119 |
C | HIS120 |
C | TYR121 |
C | TRP174 |
C | GLU177 |
C | HIS178 |
C | GLU183 |
C | HOH1005 |
C | MN4300 |
C | ZN4301 |
site_id | DC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CRN D 5401 |
Chain | Residue |
D | GLU34 |
D | HIS36 |
D | ASP45 |
D | SER78 |
D | GLY119 |
D | HIS120 |
D | TYR121 |
D | TRP154 |
D | TRP174 |
D | ASP175 |
D | GLU177 |
D | HIS178 |
D | GLU183 |
D | HOH1007 |
D | MN5300 |
D | ZN5301 |
site_id | DC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CRN E 6401 |
Chain | Residue |
E | GLU34 |
E | HIS36 |
E | ASP45 |
E | SER78 |
E | GLY119 |
E | HIS120 |
E | TYR121 |
E | TRP154 |
E | TRP174 |
E | ASP175 |
E | GLU177 |
E | HIS178 |
E | GLU183 |
E | HOH1009 |
E | MN6300 |
E | ZN6301 |
site_id | DC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CRN F 7401 |
Chain | Residue |
F | GLU34 |
F | HIS36 |
F | ASP45 |
F | SER78 |
F | GLY119 |
F | HIS120 |
F | TYR121 |
F | TRP174 |
F | ASP175 |
F | GLU177 |
F | HIS178 |
F | GLU183 |
F | HOH1011 |
F | MN7300 |
F | ZN7301 |
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 |