2CKI
Structure of Ulilysin, a member of the pappalysin family of metzincin metalloendopeptidases.
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CA A 997 | 
| Chain | Residue | 
| A | TRP240 | 
| A | GLU243 | 
| A | PRO249 | 
| A | GLN262 | 
| A | ALA263 | 
| A | HOH2243 | 
| site_id | AC2 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE CA A 998 | 
| Chain | Residue | 
| A | HOH2227 | 
| A | HOH2231 | 
| A | HOH2240 | 
| A | HOH2241 | 
| A | ASP254 | 
| A | VAL256 | 
| A | THR259 | 
| site_id | AC3 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN A 999 | 
| Chain | Residue | 
| A | HIS228 | 
| A | HIS232 | 
| A | HIS238 | 
| A | HOH2301 | 
| site_id | AC4 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CA A 1403 | 
| Chain | Residue | 
| A | ASP152 | 
| A | HOH2139 | 
| B | ASP152 | 
| B | HOH2130 | 
| B | HOH2132 | 
| B | HOH2184 | 
| site_id | AC5 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CA B 997 | 
| Chain | Residue | 
| B | TRP240 | 
| B | GLU243 | 
| B | PRO249 | 
| B | GLN262 | 
| B | ALA263 | 
| B | HOH2216 | 
| site_id | AC6 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE CA B 998 | 
| Chain | Residue | 
| B | ASP254 | 
| B | VAL256 | 
| B | THR259 | 
| B | HOH2219 | 
| B | HOH2224 | 
| B | HOH2234 | 
| B | HOH2235 | 
| site_id | AC7 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN B 999 | 
| Chain | Residue | 
| B | HIS228 | 
| B | HIS232 | 
| B | HIS238 | 
| B | HOH2289 | 
| site_id | AC8 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE GOL A 1404 | 
| Chain | Residue | 
| A | PRO68 | 
| A | THR127 | 
| A | LYS128 | 
| A | ARG169 | 
| A | TYR170 | 
| site_id | AC9 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE GOL A 1405 | 
| Chain | Residue | 
| A | ASP129 | 
| A | PRO130 | 
| A | TRP165 | 
| A | HOH2108 | 
| A | HOH2302 | 
| A | HOH2303 | 
| A | HOH2304 | 
| site_id | BC1 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE GOL A 1406 | 
| Chain | Residue | 
| A | TRP112 | 
| A | ASN282 | 
| A | HOH2268 | 
| A | HOH2305 | 
| B | GOL1404 | 
| site_id | BC2 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE GOL B 1403 | 
| Chain | Residue | 
| B | ASP129 | 
| B | PRO130 | 
| B | TRP165 | 
| B | HOH2095 | 
| B | HOH2290 | 
| B | HOH2292 | 
| site_id | BC3 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE GOL B 1404 | 
| Chain | Residue | 
| A | GOL1406 | 
| B | TRP112 | 
| B | ASN282 | 
| B | HOH2232 | 
| B | HOH2259 | 
| site_id | BC4 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE GOL B 1405 | 
| Chain | Residue | 
| B | PRO68 | 
| B | THR127 | 
| B | LYS128 | 
| B | ARG169 | 
| B | TYR170 | 
| site_id | BC5 | 
| Number of Residues | 12 | 
| Details | Binding site for Di-peptide ARG A 401 and VAL A 402 | 
| Chain | Residue | 
| A | GLN185 | 
| A | ILE187 | 
| A | LEU188 | 
| A | GLY189 | 
| A | PHE220 | 
| A | THR225 | 
| A | GLU229 | 
| A | VAL293 | 
| A | ASP295 | 
| A | HOH2299 | 
| A | HOH2300 | 
| A | HOH2301 | 
| site_id | BC6 | 
| Number of Residues | 14 | 
| Details | Binding site for Di-peptide ARG B 401 and VAL B 402 | 
| Chain | Residue | 
| B | GLN185 | 
| B | ILE187 | 
| B | LEU188 | 
| B | GLY189 | 
| B | PHE220 | 
| B | ARG224 | 
| B | THR225 | 
| B | GLU229 | 
| B | TYR292 | 
| B | VAL293 | 
| B | ASP295 | 
| B | HOH2287 | 
| B | HOH2288 | 
| B | HOH2289 | 
Functional Information from PROSITE/UniProt
| site_id | PS00142 | 
| Number of Residues | 10 | 
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TATHEIGHWL | 
| Chain | Residue | Details | 
| A | THR225-LEU234 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 2 | 
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16627477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17097044","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 2 | 
| Details | Binding site: {} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 4 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16627477","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 6 | 
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16627477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17097044","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 16 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16627477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17097044","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 











