3U4L
Cryocooled bovine profilin:actin crystal structure to 2.4 A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005884 | cellular_component | actin filament |
A | 0005886 | cellular_component | plasma membrane |
A | 0005925 | cellular_component | focal adhesion |
A | 0007409 | biological_process | axonogenesis |
A | 0015629 | cellular_component | actin cytoskeleton |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019901 | molecular_function | protein kinase binding |
A | 0030424 | cellular_component | axon |
A | 0032991 | cellular_component | protein-containing complex |
A | 0035267 | cellular_component | NuA4 histone acetyltransferase complex |
A | 0045202 | cellular_component | synapse |
A | 0048870 | biological_process | cell motility |
A | 0097433 | cellular_component | dense body |
A | 0098973 | molecular_function | structural constituent of postsynaptic actin cytoskeleton |
A | 0098974 | biological_process | postsynaptic actin cytoskeleton organization |
P | 0003779 | molecular_function | actin binding |
P | 0005737 | cellular_component | cytoplasm |
P | 0005856 | cellular_component | cytoskeleton |
P | 0030036 | biological_process | actin cytoskeleton organization |
P | 0030833 | biological_process | regulation of actin filament polymerization |
P | 0032233 | biological_process | positive regulation of actin filament bundle assembly |
P | 0044087 | biological_process | regulation of cellular component biogenesis |
P | 0110053 | biological_process | regulation of actin filament organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ATP A 401 |
Chain | Residue |
A | GLY13 |
A | GLY182 |
A | LYS213 |
A | GLU214 |
A | GLY301 |
A | GLY302 |
A | THR303 |
A | MET305 |
A | TYR306 |
A | LYS336 |
A | CA402 |
A | SER14 |
A | HOH502 |
A | HOH511 |
A | GLY15 |
A | MET16 |
A | LYS18 |
A | SER155 |
A | GLY156 |
A | ASP157 |
A | GLY158 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 402 |
Chain | Residue |
A | ATP401 |
A | HOH510 |
A | HOH511 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 403 |
Chain | Residue |
A | ASP288 |
P | ASN61 |
P | HOH210 |
Functional Information from PROSITE/UniProt
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
A | TYR53-GLY63 |
site_id | PS00414 |
Number of Residues | 9 |
Details | PROFILIN Profilin signature. xAgWNaYiD |
Chain | Residue | Details |
P | ACE0-ASP8 |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WISKqEYDE |
Chain | Residue | Details |
A | TRP356-GLU364 |
site_id | PS01132 |
Number of Residues | 13 |
Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
Chain | Residue | Details |
A | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:3342873, ECO:0000269|PubMed:446730 |
Chain | Residue | Details |
P | ALA1 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62963 |
Chain | Residue | Details |
P | SER27 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07737 |
Chain | Residue | Details |
P | SER56 | |
A | MET47 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07737 |
Chain | Residue | Details |
P | LYS107 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07737 |
Chain | Residue | Details |
P | TYR128 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by ROCK1 => ECO:0000250|UniProtKB:P07737 |
Chain | Residue | Details |
P | SER137 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07737 |
Chain | Residue | Details |
P | LYS53 |