Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0008473 | molecular_function | ornithine cyclodeaminase activity |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0055129 | biological_process | L-proline biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0008473 | molecular_function | ornithine cyclodeaminase activity |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 911 |
Chain | Residue |
A | ALA224 |
A | VAL225 |
A | GLY227 |
A | SER293 |
A | HOH992 |
A | HOH994 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 912 |
Chain | Residue |
B | SER293 |
B | HOH1104 |
B | HOH1105 |
B | ALA224 |
B | VAL225 |
B | GLY227 |
site_id | AC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD B 801 |
Chain | Residue |
A | LYS331 |
A | HOH1021 |
A | HOH1143 |
B | THR84 |
B | ARG112 |
B | THR113 |
B | GLY138 |
B | ALA139 |
B | GLN140 |
B | ASP161 |
B | THR162 |
B | VAL201 |
B | THR202 |
B | ALA203 |
B | ILE210 |
B | VAL225 |
B | GLY226 |
B | ASP228 |
B | LYS232 |
B | SER293 |
B | VAL294 |
B | GLY295 |
B | HOH1080 |
B | HOH1087 |
B | HOH1096 |
B | HOH1097 |
B | HOH1101 |
B | HOH1109 |
B | HOH1143 |
B | HOH1144 |
site_id | AC4 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD A 802 |
Chain | Residue |
A | THR84 |
A | ARG112 |
A | THR113 |
A | GLY138 |
A | ALA139 |
A | GLN140 |
A | ASP161 |
A | THR162 |
A | VAL201 |
A | THR202 |
A | ALA203 |
A | ILE210 |
A | VAL225 |
A | GLY226 |
A | ASP228 |
A | LYS232 |
A | SER293 |
A | VAL294 |
A | GLY295 |
A | HOH971 |
A | HOH973 |
A | HOH977 |
A | HOH998 |
A | HOH1002 |
A | HOH1003 |
A | HOH1004 |
A | HOH1016 |
A | HOH1018 |
A | HOH1211 |
B | LYS331 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD A 901 |
Chain | Residue |
A | GLN38 |
A | ALA39 |
A | ALA61 |
A | ASP62 |
A | LYS63 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD A 902 |
Chain | Residue |
A | ALA39 |
A | HOH1149 |
A | HOH1150 |
B | LEU216 |
B | PRO218 |
B | SER286 |
B | VAL288 |
B | HOH992 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MPD B 903 |
Chain | Residue |
B | SER64 |
B | ARG65 |
B | ALA92 |
B | ASP93 |
B | VAL100 |
B | LEU308 |
B | HOH1254 |
B | HOH1255 |
B | HOH1256 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD A 904 |
Chain | Residue |
A | TYR3 |
A | ALA311 |
A | GLU312 |
A | GLY315 |
A | MSE316 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD B 905 |
Chain | Residue |
B | TYR3 |
B | ALA311 |
B | GLU312 |
B | GLY315 |
B | MSE316 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP228 | |
B | ASP228 | |
Chain | Residue | Details |
A | ARG45 | |
A | LYS69 | |
A | ASP228 | |
A | VAL294 | |
B | ARG45 | |
B | LYS69 | |
B | ASP228 | |
B | VAL294 | |
Chain | Residue | Details |
A | THR84 | |
B | THR84 | |
B | ARG112 | |
B | ALA139 | |
B | ASP161 | |
B | THR202 | |
B | VAL225 | |
B | LYS232 | |
B | SER293 | |
B | LYS331 | |
A | ARG112 | |
A | ALA139 | |
A | ASP161 | |
A | THR202 | |
A | VAL225 | |
A | LYS232 | |
A | SER293 | |
A | LYS331 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 717 |
Chain | Residue | Details |
A | GLU56 | increase nucleophilicity, proton acceptor, proton donor |
A | ASP228 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 717 |
Chain | Residue | Details |
B | GLU56 | increase nucleophilicity, proton acceptor, proton donor |
B | ASP228 | proton acceptor, proton donor |