1HAK
CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLACENTAL ANNEXIN V COMPLEXED WITH K-201 AS A CALCIUM CHANNEL ACTIVITY INHIBITOR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001786 | molecular_function | phosphatidylserine binding |
| A | 0004859 | molecular_function | phospholipase inhibitor activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005543 | molecular_function | phospholipid binding |
| A | 0005544 | molecular_function | calcium-dependent phospholipid binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0007165 | biological_process | signal transduction |
| A | 0007596 | biological_process | blood coagulation |
| A | 0007599 | biological_process | hemostasis |
| A | 0009897 | cellular_component | external side of plasma membrane |
| A | 0012506 | cellular_component | vesicle membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0042383 | cellular_component | sarcolemma |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0050819 | biological_process | negative regulation of coagulation |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072563 | cellular_component | endothelial microparticle |
| B | 0001786 | molecular_function | phosphatidylserine binding |
| B | 0004859 | molecular_function | phospholipase inhibitor activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005544 | molecular_function | calcium-dependent phospholipid binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005925 | cellular_component | focal adhesion |
| B | 0007165 | biological_process | signal transduction |
| B | 0007596 | biological_process | blood coagulation |
| B | 0007599 | biological_process | hemostasis |
| B | 0009897 | cellular_component | external side of plasma membrane |
| B | 0012506 | cellular_component | vesicle membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0031012 | cellular_component | extracellular matrix |
| B | 0042383 | cellular_component | sarcolemma |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0050819 | biological_process | negative regulation of coagulation |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0072563 | cellular_component | endothelial microparticle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE K21 B 901 |
| Chain | Residue |
| B | LEU5 |
| B | ILE247 |
| B | ARG276 |
| B | ILE279 |
| B | THR118 |
| B | PRO119 |
| B | GLU121 |
| B | ARG161 |
| B | VAL203 |
| B | ARG207 |
| B | SER243 |
| B | ILE244 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE K21 A 901 |
| Chain | Residue |
| A | LEU5 |
| A | THR118 |
| A | PRO119 |
| A | ARG161 |
| A | VAL203 |
| A | ARG207 |
| A | SER243 |
| A | ILE244 |
Functional Information from PROSITE/UniProt
| site_id | PS00223 |
| Number of Residues | 53 |
| Details | ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfeklIvaL |
| Chain | Residue | Details |
| B | GLY32-LEU84 | |
| B | GLY104-LEU156 | |
| B | GLY188-VAL240 | |
| B | GLY263-LEU315 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 142 |
| Details | Repeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 142 |
| Details | Repeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 144 |
| Details | Repeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 142 |
| Details | Repeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Motif: {"description":"[IL]-x-C-x-x-[DE] motif","evidences":[{"source":"PubMed","id":"25417112","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P48036","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"16916647","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P48036","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
