2H0K
Crystal Structure of a Mutant of Rat Annexin A5
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001786 | molecular_function | phosphatidylserine binding |
A | 0005388 | molecular_function | P-type calcium transporter 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 | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0007596 | biological_process | blood coagulation |
A | 0008021 | cellular_component | synaptic vesicle |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0012506 | cellular_component | vesicle membrane |
A | 0014704 | cellular_component | intercalated disc |
A | 0017046 | molecular_function | peptide hormone binding |
A | 0030018 | cellular_component | Z disc |
A | 0030195 | biological_process | negative regulation of blood coagulation |
A | 0030425 | cellular_component | dendrite |
A | 0030672 | cellular_component | synaptic vesicle membrane |
A | 0030971 | molecular_function | receptor tyrosine kinase binding |
A | 0042383 | cellular_component | sarcolemma |
A | 0042802 | molecular_function | identical protein binding |
A | 0042995 | cellular_component | cell projection |
A | 0043025 | cellular_component | neuronal cell body |
A | 0043065 | biological_process | positive regulation of apoptotic process |
A | 0043204 | cellular_component | perikaryon |
A | 0043679 | cellular_component | axon terminus |
A | 0050819 | biological_process | negative regulation of coagulation |
A | 0051592 | biological_process | response to calcium ion |
A | 0070588 | biological_process | calcium ion transmembrane transport |
A | 0071284 | biological_process | cellular response to lead ion |
A | 0072563 | cellular_component | endothelial microparticle |
A | 0097066 | biological_process | response to thyroid hormone |
A | 0097211 | biological_process | cellular response to gonadotropin-releasing hormone |
A | 1901317 | biological_process | regulation of flagellated sperm motility |
A | 1902721 | biological_process | negative regulation of prolactin secretion |
B | 0001786 | molecular_function | phosphatidylserine binding |
B | 0005388 | molecular_function | P-type calcium transporter 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 | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0007596 | biological_process | blood coagulation |
B | 0008021 | cellular_component | synaptic vesicle |
B | 0009897 | cellular_component | external side of plasma membrane |
B | 0012506 | cellular_component | vesicle membrane |
B | 0014704 | cellular_component | intercalated disc |
B | 0017046 | molecular_function | peptide hormone binding |
B | 0030018 | cellular_component | Z disc |
B | 0030195 | biological_process | negative regulation of blood coagulation |
B | 0030425 | cellular_component | dendrite |
B | 0030672 | cellular_component | synaptic vesicle membrane |
B | 0030971 | molecular_function | receptor tyrosine kinase binding |
B | 0042383 | cellular_component | sarcolemma |
B | 0042802 | molecular_function | identical protein binding |
B | 0042995 | cellular_component | cell projection |
B | 0043025 | cellular_component | neuronal cell body |
B | 0043065 | biological_process | positive regulation of apoptotic process |
B | 0043204 | cellular_component | perikaryon |
B | 0043679 | cellular_component | axon terminus |
B | 0050819 | biological_process | negative regulation of coagulation |
B | 0051592 | biological_process | response to calcium ion |
B | 0070588 | biological_process | calcium ion transmembrane transport |
B | 0071284 | biological_process | cellular response to lead ion |
B | 0072563 | cellular_component | endothelial microparticle |
B | 0097066 | biological_process | response to thyroid hormone |
B | 0097211 | biological_process | cellular response to gonadotropin-releasing hormone |
B | 1901317 | biological_process | regulation of flagellated sperm motility |
B | 1902721 | biological_process | negative regulation of prolactin secretion |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 401 |
Chain | Residue |
A | MET26 |
A | GLY28 |
A | GLY30 |
A | GLU70 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 402 |
Chain | Residue |
A | LYS68 |
A | LEU71 |
A | GLU76 |
A | HOH477 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA A 403 |
Chain | Residue |
A | GLU33 |
A | THR31 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 404 |
Chain | Residue |
A | LEU98 |
A | GLY100 |
A | ALA101 |
A | THR103 |
A | ASP142 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA A 412 |
Chain | Residue |
A | THR187 |
A | GLU226 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA A 406 |
Chain | Residue |
A | THR103 |
A | GLU105 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 402 |
Chain | Residue |
B | LYS68 |
B | LEU71 |
B | GLU76 |
B | HOH451 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 403 |
Chain | Residue |
A | ASP34 |
B | THR31 |
B | GLU33 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 404 |
Chain | Residue |
B | LEU98 |
B | GLY100 |
B | ALA101 |
B | THR103 |
B | ASP142 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA B 412 |
Chain | Residue |
B | THR187 |
B | GLU226 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA B 406 |
Chain | Residue |
B | THR103 |
B | GLU105 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 409 |
Chain | Residue |
A | THR187 |
A | GLU189 |
A | HOH415 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 410 |
Chain | Residue |
A | MET257 |
A | GLY259 |
A | GLY261 |
A | ASP301 |
A | HOH416 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 408 |
Chain | Residue |
A | ASP224 |
A | THR227 |
A | GLU232 |
A | HOH417 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 407 |
Chain | Residue |
A | GLY181 |
A | LYS184 |
A | GLY186 |
A | GLU226 |
A | HOH418 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 414 |
Chain | Residue |
A | GLU93 |
A | HIS96 |
A | HIS265 |
A | HOH419 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 401 |
Chain | Residue |
B | MET26 |
B | GLY28 |
B | GLY30 |
B | GLU70 |
B | HOH415 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 409 |
Chain | Residue |
B | THR187 |
B | GLU189 |
B | HOH416 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 410 |
Chain | Residue |
B | MET257 |
B | GLY259 |
B | GLY261 |
B | ASP301 |
B | HOH417 |
B | HOH464 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 408 |
Chain | Residue |
B | ASP224 |
B | THR227 |
B | GLU232 |
B | HOH418 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 407 |
Chain | Residue |
B | GLY181 |
B | LYS184 |
B | GLY186 |
B | GLU226 |
B | HOH419 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 414 |
Chain | Residue |
B | GLU93 |
B | HIS96 |
B | HIS265 |
B | HOH420 |
Functional Information from PROSITE/UniProt
site_id | PS00223 |
Number of Residues | 53 |
Details | ANNEXIN_1 Annexin repeat signature. GTdedsilnlLtaRsnaQrqQiaeeFetlfgrdLvndMkseltGkfeklIvaL |
Chain | Residue | Details |
A | GLY30-LEU82 | |
A | GLY102-LEU154 | |
A | GLY186-VAL238 | |
A | GLY261-LEU313 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:7583670 |
Chain | Residue | Details |
A | LEU3 | |
B | LEU3 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | ILE36 | |
B | ILE36 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P08758 |
Chain | Residue | Details |
A | SER69 | |
B | GLY100 | |
A | PHE75 | |
A | LEU78 | |
A | HIS96 | |
A | GLY100 | |
B | SER69 | |
B | PHE75 | |
B | LEU78 | |
B | HIS96 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P48036 |
Chain | Residue | Details |
A | ASN289 | |
B | ASN289 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P08758 |
Chain | Residue | Details |
A | GLY28 | |
B | GLY28 |