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3UB5

Profilin:actin with a wide open nucleotide cleft

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0007409biological_processaxonogenesis
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019901molecular_functionprotein kinase binding
A0030424cellular_componentaxon
A0032991cellular_componentprotein-containing complex
A0035267cellular_componentNuA4 histone acetyltransferase complex
A0045202cellular_componentsynapse
A0048870biological_processcell motility
A0097433cellular_componentdense body
A0098973molecular_functionstructural constituent of postsynaptic actin cytoskeleton
A0098974biological_processpostsynaptic actin cytoskeleton organization
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
P0044087biological_processregulation of cellular component biogenesis
P0110053biological_processregulation of actin filament organization
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP A 376
ChainResidue
ASER14
AGLY302
AMET305
ATYR306
ALYS336
ACA377
AHOH381
AGLY15
AGLY156
AASP157
AGLY158
AGLY182
AARG210
ALYS213
AGLU214

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 377
ChainResidue
AGLY15
AMET16
AATP376

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 378
ChainResidue
ASER199
ATHR201
AGLU205

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL P 140
ChainResidue
PHIS133
PARG136

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL P 141
ChainResidue
PTYR128
PALA131
PSER132
PARG135

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
PALA1

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62963
ChainResidueDetails
PSER27
AMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PSER56

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PLYS107

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PTYR128

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ROCK1 => ECO:0000250|UniProtKB:P07737
ChainResidueDetails
PSER137

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
PLYS53

222415

PDB entries from 2024-07-10

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