Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1HLU

STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000786cellular_componentnucleosome
A0001738biological_processmorphogenesis of a polarized epithelium
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0005886cellular_componentplasma membrane
A0005903cellular_componentbrush border
A0005911cellular_componentcell-cell junction
A0005912cellular_componentadherens junction
A0005925cellular_componentfocal adhesion
A0007163biological_processestablishment or maintenance of cell polarity
A0007409biological_processaxonogenesis
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0019894molecular_functionkinesin binding
A0019901molecular_functionprotein kinase binding
A0030027cellular_componentlamellipodium
A0030235molecular_functionnitric-oxide synthase regulator activity
A0030424cellular_componentaxon
A0030863cellular_componentcortical cytoskeleton
A0030957molecular_functionTat protein binding
A0032991cellular_componentprotein-containing complex
A0034333biological_processadherens junction assembly
A0035267cellular_componentNuA4 histone acetyltransferase complex
A0036464cellular_componentcytoplasmic ribonucleoprotein granule
A0042802molecular_functionidentical protein binding
A0043296cellular_componentapical junction complex
A0044305cellular_componentcalyx of Held
A0045176biological_processapical protein localization
A0045202cellular_componentsynapse
A0048870biological_processcell motility
A0050998molecular_functionnitric-oxide synthase binding
A0051621biological_processregulation of norepinephrine uptake
A0051726biological_processregulation of cell cycle
A0070160cellular_componenttight junction
A0071896biological_processprotein localization to adherens junction
A0072749biological_processcellular response to cytochalasin B
A0097433cellular_componentdense body
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098871cellular_componentpostsynaptic actin cytoskeleton
A0098973molecular_functionstructural constituent of postsynaptic actin cytoskeleton
A0098974biological_processpostsynaptic actin cytoskeleton organization
A0098978cellular_componentglutamatergic synapse
A0141108molecular_functiontransporter regulator activity
A0150111biological_processregulation of transepithelial transport
A1900242biological_processregulation of synaptic vesicle endocytosis
A1903076biological_processregulation of protein localization to plasma membrane
A1905168biological_processpositive regulation of double-strand break repair via homologous recombination
A1990904cellular_componentribonucleoprotein complex
P0003779molecular_functionactin binding
P0005737cellular_componentcytoplasm
P0005856cellular_componentcytoskeleton
P0030036biological_processactin cytoskeleton organization
P0030833biological_processregulation of actin filament polymerization
P0032233biological_processpositive regulation of actin filament bundle assembly
P0110053biological_processregulation of actin filament organization
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 376
ChainResidue
AATP1

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP A 1
ChainResidue
ASER14
AGLY15
AMET16
AGLY156
AASP157
AGLY158
AGLY182
AARG210
ALYS213
AGLU214
AGLY302
ATHR303
AMET305
ACA376

site_idCAT
Number of Residues1
DetailsCALCIUM (DIVALENT CATION) BINDING SITE WITH ATP. UNLIKE PDB ENTRY 2BTF, DIVALENT CATION ONLY MAKES SIGNIFICANT CONTACT WITH ATP PHOSPHATES.
ChainResidue
AATP1

site_idNUC
Number of Residues9
DetailsATP BINDING SITE, TAKEN FROM PDB ENTRY 2BTF.
ChainResidue
AGLY302
ASER14
AGLY15
AMET16
ALYS18
AASP157
AGLY158
AVAL159
AGLU214

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00414
Number of Residues9
DetailsPROFILIN Profilin signature. xAgWNaYiD
ChainResidueDetails
PACE0-ASP8

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WISKqEYDE
ChainResidueDetails
ATRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:3342873, ECO:0000269|PubMed:446730
ChainResidueDetails
PGLY2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62963
ChainResidueDetails
PPRO28
AMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PSER57

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PTHR108

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PGLU129

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ROCK1 => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PGLN138

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PASP54

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon