1RTP
REFINED X-RAY STRUCTURE OF RAT PARVALBUMIN, A MAMMALIAN ALPHA-LINEAGE PARVALBUMIN, AT 2.0 A RESOLUTION
Functional Information from GO Data
Chain | GOid | namespace | contents |
1 | 0005509 | molecular_function | calcium ion binding |
1 | 0005737 | cellular_component | cytoplasm |
1 | 0010467 | biological_process | gene expression |
1 | 0030424 | cellular_component | axon |
1 | 0032420 | cellular_component | stereocilium |
1 | 0032437 | cellular_component | cuticular plate |
1 | 0032991 | cellular_component | protein-containing complex |
1 | 0042802 | molecular_function | identical protein binding |
1 | 0043025 | cellular_component | neuronal cell body |
1 | 0043195 | cellular_component | terminal bouton |
1 | 0044877 | molecular_function | protein-containing complex binding |
1 | 0046872 | molecular_function | metal ion binding |
1 | 0090102 | biological_process | cochlea development |
1 | 0098976 | biological_process | excitatory chemical synaptic transmission |
1 | 0098977 | biological_process | inhibitory chemical synaptic transmission |
2 | 0005509 | molecular_function | calcium ion binding |
2 | 0005737 | cellular_component | cytoplasm |
2 | 0010467 | biological_process | gene expression |
2 | 0030424 | cellular_component | axon |
2 | 0032420 | cellular_component | stereocilium |
2 | 0032437 | cellular_component | cuticular plate |
2 | 0032991 | cellular_component | protein-containing complex |
2 | 0042802 | molecular_function | identical protein binding |
2 | 0043025 | cellular_component | neuronal cell body |
2 | 0043195 | cellular_component | terminal bouton |
2 | 0044877 | molecular_function | protein-containing complex binding |
2 | 0046872 | molecular_function | metal ion binding |
2 | 0090102 | biological_process | cochlea development |
2 | 0098976 | biological_process | excitatory chemical synaptic transmission |
2 | 0098977 | biological_process | inhibitory chemical synaptic transmission |
3 | 0005509 | molecular_function | calcium ion binding |
3 | 0005737 | cellular_component | cytoplasm |
3 | 0010467 | biological_process | gene expression |
3 | 0030424 | cellular_component | axon |
3 | 0032420 | cellular_component | stereocilium |
3 | 0032437 | cellular_component | cuticular plate |
3 | 0032991 | cellular_component | protein-containing complex |
3 | 0042802 | molecular_function | identical protein binding |
3 | 0043025 | cellular_component | neuronal cell body |
3 | 0043195 | cellular_component | terminal bouton |
3 | 0044877 | molecular_function | protein-containing complex binding |
3 | 0046872 | molecular_function | metal ion binding |
3 | 0090102 | biological_process | cochlea development |
3 | 0098976 | biological_process | excitatory chemical synaptic transmission |
3 | 0098977 | biological_process | inhibitory chemical synaptic transmission |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA 1 110 |
Chain | Residue |
1 | ASP51 |
1 | ASP53 |
1 | SER55 |
1 | PHE57 |
1 | GLU59 |
1 | GLU62 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA 1 111 |
Chain | Residue |
1 | ASP90 |
1 | ASP92 |
1 | ASP94 |
1 | LYS96 |
1 | GLU101 |
1 | HOH121 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA 2 110 |
Chain | Residue |
2 | ASP51 |
2 | ASP53 |
2 | SER55 |
2 | PHE57 |
2 | GLU59 |
2 | GLU62 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA 2 111 |
Chain | Residue |
2 | ASP90 |
2 | ASP92 |
2 | ASP94 |
2 | LYS96 |
2 | GLU101 |
2 | HOH148 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA 3 110 |
Chain | Residue |
3 | ASP51 |
3 | ASP53 |
3 | SER55 |
3 | PHE57 |
3 | GLU59 |
3 | GLU62 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA 3 111 |
Chain | Residue |
3 | ASP90 |
3 | ASP92 |
3 | ASP94 |
3 | LYS96 |
3 | GLU101 |
3 | HOH145 |
site_id | CA1 |
Number of Residues | 6 |
Details |
Chain | Residue |
1 | ASP51 |
1 | ASP53 |
1 | SER55 |
1 | PHE57 |
1 | GLU59 |
1 | GLU62 |
site_id | CA2 |
Number of Residues | 6 |
Details |
Chain | Residue |
1 | LYS96 |
1 | GLU101 |
1 | HOH121 |
1 | ASP90 |
1 | ASP92 |
1 | ASP94 |
site_id | CB1 |
Number of Residues | 6 |
Details |
Chain | Residue |
2 | ASP51 |
2 | ASP53 |
2 | SER55 |
2 | PHE57 |
2 | GLU59 |
2 | GLU62 |
site_id | CB2 |
Number of Residues | 6 |
Details |
Chain | Residue |
2 | ASP90 |
2 | ASP92 |
2 | ASP94 |
2 | LYS96 |
2 | GLU101 |
1 | HOH121 |
site_id | CC1 |
Number of Residues | 6 |
Details |
Chain | Residue |
3 | ASP51 |
3 | ASP53 |
3 | SER55 |
3 | PHE57 |
3 | GLU59 |
3 | GLU62 |
site_id | CC2 |
Number of Residues | 6 |
Details |
Chain | Residue |
3 | ASP90 |
3 | ASP92 |
3 | ASP94 |
3 | LYS96 |
3 | GLU101 |
1 | HOH121 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DKDKSGFIEedEL |
Chain | Residue | Details |
1 | ASP51-LEU63 | |
1 | ASP90-PHE102 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 27 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
Chain | Residue | Details |
1 | LYS52 | |
2 | LYS52 | |
2 | LYS54 | |
2 | GLY56 | |
2 | LEU63 | |
2 | LYS91 | |
2 | GLY93 | |
2 | GLY95 | |
2 | ILE97 | |
2 | PHE102 | |
3 | LYS52 | |
1 | LYS54 | |
3 | LYS54 | |
3 | GLY56 | |
3 | LEU63 | |
3 | LYS91 | |
3 | GLY93 | |
3 | GLY95 | |
3 | ILE97 | |
3 | PHE102 | |
1 | GLY56 | |
1 | LEU63 | |
1 | LYS91 | |
1 | GLY93 | |
1 | GLY95 | |
1 | ILE97 | |
1 | PHE102 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
1 | MET2 | |
3 | ALA8 | |
3 | PHE24 | |
3 | ILE66 | |
1 | ALA8 | |
1 | PHE24 | |
1 | ILE66 | |
2 | MET2 | |
2 | ALA8 | |
2 | PHE24 | |
2 | ILE66 | |
3 | MET2 |