2ZNH
Crystal Structure of a Domain-Swapped Serpin Dimer
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 | 0005788 | cellular_component | endoplasmic reticulum lumen |
A | 0005886 | cellular_component | plasma membrane |
A | 0007596 | biological_process | blood coagulation |
A | 0008201 | molecular_function | heparin binding |
A | 0010466 | biological_process | negative regulation of peptidase activity |
A | 0030193 | biological_process | regulation of blood coagulation |
A | 0042802 | molecular_function | identical protein binding |
A | 0062023 | cellular_component | collagen-containing extracellular matrix |
A | 0070062 | cellular_component | extracellular exosome |
A | 0072562 | cellular_component | blood microparticle |
B | 0002020 | molecular_function | protease binding |
B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005788 | cellular_component | endoplasmic reticulum lumen |
B | 0005886 | cellular_component | plasma membrane |
B | 0007596 | biological_process | blood coagulation |
B | 0008201 | molecular_function | heparin binding |
B | 0010466 | biological_process | negative regulation of peptidase activity |
B | 0030193 | biological_process | regulation of blood coagulation |
B | 0042802 | molecular_function | identical protein binding |
B | 0062023 | cellular_component | collagen-containing extracellular matrix |
B | 0070062 | cellular_component | extracellular exosome |
B | 0072562 | cellular_component | blood microparticle |
Functional Information from PROSITE/UniProt
site_id | PS00284 |
Number of Residues | 11 |
Details | SERPIN Serpins signature. FKANRPFLVfI |
Chain | Residue | Details |
A | PHE402-ILE412 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | TRP49 | |
A | ARG129 | |
A | ARG145 | |
B | TRP49 | |
B | ARG129 | |
B | ARG145 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Reactive bond => ECO:0000269|PubMed:7238875 |
Chain | Residue | Details |
A | ARG393 | |
B | ARG393 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039 |
Chain | Residue | Details |
A | THR31 | |
B | THR31 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER36 | |
B | SER36 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.10 |
Chain | Residue | Details |
A | ASN96 | |
B | ASN96 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.10 |
Chain | Residue | Details |
A | ASN135 | |
B | ASN135 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|Ref.10 |
Chain | Residue | Details |
A | ASN155 | |
B | ASN155 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10 |
Chain | Residue | Details |
A | ASN192 | |
B | ASN192 |