1HP7
A 2.1 ANGSTROM STRUCTURE OF AN UNCLEAVED ALPHA-1-ANTITRYPSIN SHOWS VARIABILITY OF THE REACTIVE CENTER AND OTHER LOOPS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002020 | molecular_function | protease binding |
| A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006953 | biological_process | acute-phase response |
| A | 0007596 | biological_process | blood coagulation |
| A | 0007599 | biological_process | hemostasis |
| A | 0030134 | cellular_component | COPII-coated ER to Golgi transport vesicle |
| A | 0030414 | molecular_function | peptidase inhibitor activity |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0031093 | cellular_component | platelet alpha granule lumen |
| A | 0033116 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS73 |
| A | GLU89 |
| A | HIS93 |
| A | HOH486 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | GLU151 |
| A | GLU175 |
| A | HIS231 |
| A | ASP256 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 403 |
| Chain | Residue |
| A | HIS262 |
| A | HOH438 |
| A | HIS43 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 404 |
| Chain | Residue |
| A | SER285 |
| A | HIS287 |
| A | GLU324 |
| A | GLU363 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 405 |
| Chain | Residue |
| A | GLU98 |
| A | HIS101 |
| A | HIS139 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 432 |
| Chain | Residue |
| A | CYS232 |
| A | LYS233 |
Functional Information from PROSITE/UniProt
| site_id | PS00284 |
| Number of Residues | 11 |
| Details | SERPIN Serpins signature. VKFNKPFVFlM |
| Chain | Residue | Details |
| A | VAL364-MET374 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 43 |
| Details | Peptide: {"description":"Short peptide from AAT","featureId":"PRO_0000364030"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Region: {"description":"RCL"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur","evidences":[{"source":"PubMed","id":"3533918","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases","evidences":[{"source":"PubMed","id":"3533918","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-cysteinyl cysteine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16622833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16622833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16622833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
