3A6D
Creatininase complexed with 1-methylguanidine
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 | HOH2083 |
A | HOH2087 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | MN300 |
A | HOH2087 |
A | HIS36 |
A | ASP45 |
A | GLU183 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MGX A 302 |
Chain | Residue |
A | SER78 |
A | TRP174 |
A | ASP175 |
A | GLU177 |
A | HIS178 |
A | HOH1205 |
A | HOH2083 |
A | HOH2087 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 404 |
Chain | Residue |
A | ARG113 |
A | LYS147 |
A | GLU256 |
A | PHE257 |
A | HOH1408 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 410 |
Chain | Residue |
A | LYS54 |
A | ARG55 |
A | TYR191 |
A | HOH1334 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 416 |
Chain | Residue |
A | ARG59 |
A | GLN247 |
A | ARG254 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 300 |
Chain | Residue |
B | GLU34 |
B | ASP45 |
B | HIS120 |
B | ZN301 |
B | HOH2084 |
B | HOH2088 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 301 |
Chain | Residue |
B | HIS36 |
B | ASP45 |
B | GLU183 |
B | MN300 |
B | HOH2088 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MGX B 303 |
Chain | Residue |
B | SER78 |
B | TRP174 |
B | ASP175 |
B | GLU177 |
B | HOH1167 |
B | HOH2084 |
B | HOH2088 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 405 |
Chain | Residue |
B | ARG113 |
B | GLU256 |
B | PHE257 |
B | HOH1505 |
B | HOH1651 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 411 |
Chain | Residue |
B | LYS54 |
B | ARG55 |
B | TYR191 |
B | HOH1350 |
B | HOH1803 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 417 |
Chain | Residue |
B | ARG59 |
B | GLN247 |
B | ARG254 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 300 |
Chain | Residue |
C | GLU34 |
C | ASP45 |
C | HIS120 |
C | ZN301 |
C | HOH1324 |
C | HOH2085 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 301 |
Chain | Residue |
C | HIS36 |
C | ASP45 |
C | GLU183 |
C | MN300 |
C | HOH1324 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MGX C 304 |
Chain | Residue |
C | SER78 |
C | TRP174 |
C | ASP175 |
C | GLU177 |
C | HOH1242 |
C | HOH1324 |
C | HOH2085 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 406 |
Chain | Residue |
C | ARG113 |
C | LYS147 |
C | GLU256 |
C | PHE257 |
C | HOH1484 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 412 |
Chain | Residue |
C | LYS54 |
C | ARG55 |
C | TYR191 |
C | HOH1331 |
C | HOH1819 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 418 |
Chain | Residue |
C | ARG59 |
C | GLN247 |
C | ARG254 |
site_id | CC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN D 300 |
Chain | Residue |
D | HOH1657 |
D | GLU34 |
D | ASP45 |
D | HIS120 |
D | ZN301 |
D | HOH1028 |
D | HOH1129 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 301 |
Chain | Residue |
D | HIS36 |
D | ASP45 |
D | GLU183 |
D | MN300 |
D | HOH1657 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MGX D 305 |
Chain | Residue |
D | SER78 |
D | TRP174 |
D | ASP175 |
D | HIS178 |
D | HOH1028 |
D | HOH1129 |
D | HOH1657 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 401 |
Chain | Residue |
D | ARG59 |
D | GLN247 |
D | ARG254 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 407 |
Chain | Residue |
D | ARG113 |
D | LYS147 |
D | GLU256 |
D | PHE257 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 413 |
Chain | Residue |
D | LYS54 |
D | ARG55 |
D | TYR191 |
D | HOH1360 |
site_id | CC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN E 300 |
Chain | Residue |
E | GLU34 |
E | ASP45 |
E | HIS120 |
E | ZN301 |
E | HOH1076 |
E | HOH1326 |
E | HOH1477 |
site_id | CC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 301 |
Chain | Residue |
E | HIS36 |
E | ASP45 |
E | GLU183 |
E | MN300 |
E | HOH1326 |
site_id | CC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MGX E 306 |
Chain | Residue |
E | SER78 |
E | TRP174 |
E | ASP175 |
E | GLU177 |
E | HOH1076 |
E | HOH1326 |
E | HOH1477 |
site_id | DC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 402 |
Chain | Residue |
E | ARG59 |
E | GLN247 |
E | ARG254 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 408 |
Chain | Residue |
E | ARG113 |
E | GLU256 |
E | PHE257 |
E | PRO258 |
E | HOH1487 |
site_id | DC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 414 |
Chain | Residue |
E | LYS54 |
E | ARG55 |
E | TYR191 |
E | HOH1345 |
E | HOH2082 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 300 |
Chain | Residue |
F | GLU34 |
F | ASP45 |
F | HIS120 |
F | ZN301 |
F | HOH2086 |
F | HOH2089 |
site_id | DC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 301 |
Chain | Residue |
F | HIS36 |
F | ASP45 |
F | GLU183 |
F | MN300 |
F | HOH2089 |
site_id | DC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MGX F 307 |
Chain | Residue |
F | SER78 |
F | TRP174 |
F | ASP175 |
F | GLU177 |
F | HOH1469 |
F | HOH2086 |
F | HOH2089 |
site_id | DC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 F 403 |
Chain | Residue |
F | ARG59 |
F | GLN247 |
F | ARG254 |
site_id | DC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 F 409 |
Chain | Residue |
F | ARG113 |
F | LYS147 |
F | GLU256 |
F | PHE257 |
F | HOH1567 |
site_id | DC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 F 415 |
Chain | Residue |
F | LYS54 |
F | ARG55 |
F | TYR191 |
F | HOH1357 |
F | HOH2007 |
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 |
B | GLU34 | |
A | HIS120 | |
E | HIS120 | |
F | GLU34 | |
F | HIS120 | |
D | GLU34 | |
D | HIS120 | |
E | GLU34 | |
B | HIS120 | |
C | GLU34 | |
C | HIS120 | |
A | 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 | |
A | ASP45 | |
D | HIS36 | |
D | ASP45 | |
D | GLU183 | |
E | HIS36 | |
E | ASP45 | |
E | GLU183 | |
F | HIS36 | |
F | ASP45 | |
F | GLU183 | |
C | HIS36 | |
C | ASP45 | |
C | GLU183 | |
A | GLU183 | |
B | HIS36 | |
B | ASP45 | |
B | 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 |
B | TYR121 | |
B | TRP174 | |
B | ASP175 | |
B | HIS178 | |
C | SER78 | |
C | TYR121 | |
C | TRP174 | |
C | ASP175 | |
C | HIS178 | |
D | SER78 | |
D | TYR121 | |
D | TRP174 | |
D | ASP175 | |
D | HIS178 | |
E | SER78 | |
E | TYR121 | |
E | TRP174 | |
E | ASP175 | |
E | HIS178 | |
F | SER78 | |
F | TYR121 | |
F | TRP174 | |
F | ASP175 | |
F | HIS178 | |
A | SER78 | |
A | TYR121 | |
A | TRP174 | |
A | ASP175 | |
A | HIS178 | |
B | SER78 |
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 |