1X7D
Crystal Structure Analysis of Ornithine Cyclodeaminase Complexed with NAD and ornithine to 1.6 Angstroms
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 1501 |
| Chain | Residue |
| A | ALA224 |
| A | VAL225 |
| A | GLY227 |
| A | SER293 |
| A | HOH1513 |
| A | HOH1879 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 1502 |
| Chain | Residue |
| B | SER293 |
| B | HOH3176 |
| B | HOH3315 |
| B | ALA224 |
| B | VAL225 |
| B | GLY227 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 1301 |
| Chain | Residue |
| A | LYS331 |
| A | ORN1102 |
| A | HOH1516 |
| A | HOH1668 |
| 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 | HOH3165 |
| B | HOH3166 |
| B | HOH3170 |
| B | HOH3209 |
| B | HOH3223 |
| B | HOH3323 |
| B | HOH3387 |
| B | HOH3538 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 1302 |
| 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 | ORN1101 |
| A | HOH1503 |
| A | HOH1504 |
| A | HOH1512 |
| A | HOH1519 |
| A | HOH1559 |
| A | HOH1598 |
| A | HOH1610 |
| A | HOH1686 |
| A | HOH1695 |
| A | HOH1801 |
| B | LYS331 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ORN A 1101 |
| Chain | Residue |
| A | ARG45 |
| A | VAL54 |
| A | GLU56 |
| A | LYS69 |
| A | VAL71 |
| A | ASN72 |
| A | GLY73 |
| A | VAL85 |
| A | ARG112 |
| A | ASP228 |
| A | VAL294 |
| A | GLY295 |
| A | NAD1302 |
| A | HOH1558 |
| A | HOH1642 |
| A | HOH1695 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ORN A 1102 |
| Chain | Residue |
| B | ARG112 |
| B | ASP228 |
| B | VAL294 |
| B | GLY295 |
| B | NAD1301 |
| B | HOH3207 |
| A | HOH1611 |
| B | ARG45 |
| B | VAL54 |
| B | GLU56 |
| B | MSE58 |
| B | LYS69 |
| B | ASN72 |
| B | GLY73 |
| B | VAL85 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES B 3158 |
| Chain | Residue |
| A | GLN283 |
| A | SER284 |
| A | GLN287 |
| A | ARG338 |
| A | HOH1793 |
| B | HIS15 |
| B | GLU176 |
| B | TYR177 |
| B | HOH3259 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 1401 |
| Chain | Residue |
| A | GLN38 |
| A | ALA39 |
| A | PHE40 |
| A | ASP62 |
| A | LYS63 |
| A | MPD1402 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD A 1402 |
| Chain | Residue |
| A | GLN38 |
| A | ALA39 |
| A | MPD1401 |
| B | LEU216 |
| B | ASN242 |
| B | SER286 |
| B | HOH3440 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 1403 |
| Chain | Residue |
| A | SER64 |
| A | ARG65 |
| A | LEU91 |
| A | ASP93 |
| A | VAL100 |
| A | HOH1592 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1404 |
| Chain | Residue |
| A | TYR3 |
| A | ALA311 |
| A | GLU312 |
| A | MSE316 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B 1405 |
| Chain | Residue |
| B | TYR3 |
| B | ALA311 |
| B | GLU312 |
| B | GLY315 |
| B | MSE316 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD B 1406 |
| Chain | Residue |
| B | SER64 |
| B | ARG65 |
| B | ALA92 |
| B | ASP93 |
| B | VAL100 |
| B | LEU308 |
| B | HOH3267 |
| B | HOH3513 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15518536","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1X7D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15518536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1X7D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15518536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X7D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 15518536 |
| Chain | Residue | Details |
| A | ASP228 | |
| A | GLU56 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 15518536 |
| Chain | Residue | Details |
| B | ASP228 | |
| B | GLU56 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 717 |
| Chain | Residue | Details |
| A | VAL60 | increase nucleophilicity, proton acceptor, proton donor |
| A | GLU256 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 717 |
| Chain | Residue | Details |
| B | VAL60 | increase nucleophilicity, proton acceptor, proton donor |
| B | GLU256 | proton acceptor, proton donor |
