1OO8
CRYSTAL STRUCTURE OF A1PI-PITTSBURGH IN THE NATIVE CONFORMATION
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 | 0010466 | biological_process | negative regulation of peptidase activity |
A | 0030134 | cellular_component | COPII-coated ER to Golgi transport vesicle |
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 PROSITE/UniProt
site_id | PS00284 |
Number of Residues | 11 |
Details | SERPIN Serpins signature. VKFNKPFVFlI |
Chain | Residue | Details |
A | VAL364-ILE374 |
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 | ARG358 |
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 | SER232 |
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 |