1AXN
THE HIGH RESOLUTION STRUCTURE OF ANNEXIN III SHOWS DIFFERENCES WITH ANNEXIN V
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 | 0005544 | molecular_function | calcium-dependent phospholipid binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006909 | biological_process | phagocytosis |
| A | 0010595 | biological_process | positive regulation of endothelial cell migration |
| A | 0012506 | cellular_component | vesicle membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0019834 | molecular_function | phospholipase A2 inhibitor activity |
| A | 0030670 | cellular_component | phagocytic vesicle membrane |
| A | 0042581 | cellular_component | specific granule |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0043312 | biological_process | neutrophil degranulation |
| A | 0045766 | biological_process | positive regulation of angiogenesis |
| A | 0048306 | molecular_function | calcium-dependent protein binding |
| A | 0051091 | biological_process | positive regulation of DNA-binding transcription factor activity |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 351 |
| Chain | Residue |
| A | ILE32 |
| A | GLY34 |
| A | GLY36 |
| A | THR37 |
| A | ASP76 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 352 |
| Chain | Residue |
| A | GLU148 |
| A | MET104 |
| A | GLY106 |
| A | GLY108 |
| A | THR109 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 353 |
| Chain | Residue |
| A | GLY187 |
| A | ARG190 |
| A | GLY192 |
| A | GLU232 |
| A | HOH406 |
| A | HOH407 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 354 |
| Chain | Residue |
| A | LYS230 |
| A | LEU233 |
| A | GLU238 |
| A | HOH580 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 355 |
| Chain | Residue |
| A | THR193 |
| A | GLU195 |
| A | HOH458 |
| A | HOH603 |
Functional Information from PROSITE/UniProt
| site_id | PS00223 |
| Number of Residues | 53 |
| Details | ANNEXIN_1 Annexin repeat signature. GTdekmlisiLteRsnaQrqLivkeYqaaygkeLkddLkgdlsGhfehlMvaL |
| Chain | Residue | Details |
| A | GLY36-LEU88 | |
| A | GLY108-LEU160 | |
| A | GLY192-ILE244 | |
| A | GLY267-ILE319 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 71 |
| 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 | 71 |
| 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 | 72 |
| 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 | 71 |
| 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 | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Heiserich L.","Gottlieb E."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14669","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
