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 | 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 | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0062023 | cellular_component | collagen-containing extracellular matrix |
| 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 | 1 |
| Details | SITE: (Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur => ECO:0000269|PubMed:3533918 |
| Chain | Residue | Details |
| A | LYS328 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | SITE: (Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases => ECO:0000269|PubMed:3533918 |
| Chain | Residue | Details |
| A | SER330 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Reactive bond |
| Chain | Residue | Details |
| A | MET358 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 |
| Chain | Residue | Details |
| A | SER14 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: S-cysteinyl cysteine |
| Chain | Residue | Details |
| A | CYS232 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER359 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320 |
| Chain | Residue | Details |
| A | ASN46 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169 |
| Chain | Residue | Details |
| A | ASN83 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320 |
| Chain | Residue | Details |
| A | ASN247 |
