1ANX
THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF 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 | 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 | 0009897 | cellular_component | external side of plasma membrane |
A | 0012506 | cellular_component | vesicle membrane |
A | 0016020 | cellular_component | membrane |
A | 0042383 | cellular_component | sarcolemma |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0050819 | biological_process | negative regulation of coagulation |
A | 0062023 | cellular_component | collagen-containing extracellular matrix |
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 | 0009897 | cellular_component | external side of plasma membrane |
B | 0012506 | cellular_component | vesicle membrane |
B | 0016020 | cellular_component | membrane |
B | 0042383 | cellular_component | sarcolemma |
B | 0043066 | biological_process | negative regulation of apoptotic process |
B | 0050819 | biological_process | negative regulation of coagulation |
B | 0062023 | cellular_component | collagen-containing extracellular matrix |
B | 0070062 | cellular_component | extracellular exosome |
B | 0072563 | cellular_component | endothelial microparticle |
C | 0001786 | molecular_function | phosphatidylserine binding |
C | 0004859 | molecular_function | phospholipase inhibitor activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005543 | molecular_function | phospholipid binding |
C | 0005544 | molecular_function | calcium-dependent phospholipid binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005925 | cellular_component | focal adhesion |
C | 0007165 | biological_process | signal transduction |
C | 0007596 | biological_process | blood coagulation |
C | 0009897 | cellular_component | external side of plasma membrane |
C | 0012506 | cellular_component | vesicle membrane |
C | 0016020 | cellular_component | membrane |
C | 0042383 | cellular_component | sarcolemma |
C | 0043066 | biological_process | negative regulation of apoptotic process |
C | 0050819 | biological_process | negative regulation of coagulation |
C | 0062023 | cellular_component | collagen-containing extracellular matrix |
C | 0070062 | cellular_component | extracellular exosome |
C | 0072563 | cellular_component | endothelial microparticle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 321 |
Chain | Residue |
A | GLY183 |
A | LYS186 |
A | GLY188 |
A | GLU228 |
A | SO4322 |
A | HOH326 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 322 |
Chain | Residue |
A | THR189 |
A | GLU228 |
A | CA321 |
A | HOH339 |
A | HOH420 |
A | HOH449 |
B | GLN181 |
A | LYS186 |
A | TRP187 |
A | GLY188 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 323 |
Chain | Residue |
A | MET28 |
A | GLY30 |
A | GLY32 |
A | GLU72 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 324 |
Chain | Residue |
A | LYS70 |
A | LEU73 |
A | GLU78 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 325 |
Chain | Residue |
A | ASP226 |
A | THR229 |
A | GLU234 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 321 |
Chain | Residue |
B | GLY183 |
B | LYS186 |
B | GLY188 |
B | GLU228 |
B | SO4322 |
B | HOH345 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 322 |
Chain | Residue |
B | LYS186 |
B | GLY188 |
B | THR189 |
B | GLU228 |
B | CA321 |
B | HOH345 |
B | HOH362 |
B | HOH382 |
C | GLN181 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 323 |
Chain | Residue |
B | MET28 |
B | GLY30 |
B | GLY32 |
B | GLU72 |
B | HOH441 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 324 |
Chain | Residue |
B | LYS70 |
B | LEU73 |
B | GLU78 |
B | HOH455 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 325 |
Chain | Residue |
B | ASP226 |
B | THR229 |
B | GLU234 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 321 |
Chain | Residue |
C | GLY183 |
C | LYS186 |
C | GLY188 |
C | GLU228 |
C | SO4322 |
C | HOH333 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 C 322 |
Chain | Residue |
A | GLN181 |
C | LYS186 |
C | TRP187 |
C | GLY188 |
C | THR189 |
C | GLU228 |
C | CA321 |
C | HOH441 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA C 323 |
Chain | Residue |
C | MET28 |
C | GLY30 |
C | GLY32 |
C | GLU72 |
C | HOH385 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA C 324 |
Chain | Residue |
C | LYS70 |
C | LEU73 |
C | GLU78 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA C 325 |
Chain | Residue |
C | ASP226 |
C | THR229 |
C | GLU234 |
Functional Information from PROSITE/UniProt
site_id | PS00223 |
Number of Residues | 53 |
Details | ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfeklIvaL |
Chain | Residue | Details |
A | GLY32-LEU84 | |
A | GLY104-LEU156 | |
A | GLY188-VAL240 | |
A | GLY263-LEU315 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | GLN3 | |
B | GLN3 | |
C | GLN3 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48036 |
Chain | Residue | Details |
A | ILE38 | |
B | ILE38 | |
C | ILE38 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | SER71 | |
C | PHE77 | |
C | LEU80 | |
C | HIS98 | |
A | PHE77 | |
A | LEU80 | |
A | HIS98 | |
B | SER71 | |
B | PHE77 | |
B | LEU80 | |
B | HIS98 | |
C | SER71 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:16916647 |
Chain | Residue | Details |
A | GLY102 | |
B | GLY102 | |
C | GLY102 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P48036 |
Chain | Residue | Details |
A | ASN291 | |
B | ASN291 | |
C | ASN291 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | GLY30 | |
B | GLY30 | |
C | GLY30 |