4ORY
Three-dimensional structure of the C65A-K59A double mutant of Human lipocalin-type Prostaglandin D Synthase holo, second crystal form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0036094 | molecular_function | small molecule binding |
| B | 0036094 | molecular_function | small molecule binding |
| C | 0036094 | molecular_function | small molecule binding |
| D | 0036094 | molecular_function | small molecule binding |
| E | 0036094 | molecular_function | small molecule binding |
| F | 0036094 | molecular_function | small molecule binding |
| G | 0036094 | molecular_function | small molecule binding |
| H | 0036094 | molecular_function | small molecule binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE PEU E 201 |
| Chain | Residue |
| E | ASN51 |
| E | MET145 |
| F | SER45 |
| F | LEU48 |
| F | ASN51 |
| F | SER52 |
| F | LEU55 |
| F | LEU79 |
| F | ARG92 |
| F | MET94 |
| F | SER133 |
| E | SER52 |
| F | PRO139 |
| F | PHE143 |
| F | MET145 |
| F | THR147 |
| F | HOH208 |
| E | LEU55 |
| E | ARG92 |
| E | MET94 |
| E | TYR107 |
| E | TRP112 |
| E | SER133 |
| E | PHE143 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE PEU G 201 |
| Chain | Residue |
| G | SER45 |
| G | ASN51 |
| G | SER52 |
| G | LEU55 |
| G | ALA59 |
| G | ARG92 |
| G | MET94 |
| G | TRP112 |
| G | TYR116 |
| G | VAL118 |
| G | SER133 |
| G | PHE143 |
| G | MET145 |
| G | THR147 |
| G | HOH317 |
| H | ASN51 |
| H | SER52 |
| H | LEU62 |
| H | ARG92 |
| H | SER133 |
| H | ASP142 |
| H | MET145 |
| H | HOH215 |
Functional Information from PROSITE/UniProt
| site_id | PS00213 |
| Number of Residues | 14 |
| Details | LIPOCALIN Lipocalin signature. NFQqdKFLGRWFSA |
| Chain | Residue | Details |
| A | ASN33-ALA46 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20667974","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"23234360","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8336134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8336134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
