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3U9D

Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0001725cellular_componentstress fiber
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0009612biological_processresponse to mechanical stimulus
A0010628biological_processpositive regulation of gene expression
A0015629cellular_componentactin cytoskeleton
A0016787molecular_functionhydrolase activity
A0030017cellular_componentsarcomere
A0030027cellular_componentlamellipodium
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0035865biological_processcellular response to potassium ion
A0043503biological_processskeletal muscle fiber adaptation
A0044297cellular_componentcell body
A0048545biological_processresponse to steroid hormone
A0048741biological_processskeletal muscle fiber development
A0090131biological_processmesenchyme migration
B0003785molecular_functionactin monomer binding
B0007015biological_processactin filament organization
C0001725cellular_componentstress fiber
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0009612biological_processresponse to mechanical stimulus
C0010628biological_processpositive regulation of gene expression
C0015629cellular_componentactin cytoskeleton
C0016787molecular_functionhydrolase activity
C0030017cellular_componentsarcomere
C0030027cellular_componentlamellipodium
C0030175cellular_componentfilopodium
C0030240biological_processskeletal muscle thin filament assembly
C0035865biological_processcellular response to potassium ion
C0043503biological_processskeletal muscle fiber adaptation
C0044297cellular_componentcell body
C0048545biological_processresponse to steroid hormone
C0048741biological_processskeletal muscle fiber development
C0090131biological_processmesenchyme migration
D0003785molecular_functionactin monomer binding
D0007015biological_processactin filament organization
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP A 501
ChainResidue
AGLY13
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
AMG502
ASER14
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AGLN137
AATP501

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP C 501
ChainResidue
CGLY13
CSER14
CGLY15
CLEU16
CLYS18
CGLN137
CASP154
CGLY156
CASP157
CGLY182
CLYS213
CGLU214
CGLY302
CTHR303
CMET305
CTYR306
CLYS336
CMG502

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 502
ChainResidue
CASP11
CGLY13
CGLN137
CATP501

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

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

site_idPS00500
Number of Residues12
DetailsTHYMOSIN_B4 Thymosin beta-4 family signature. LKKTETqeKNPL
ChainResidueDetails
BLEU30-LEU41

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 Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62328
ChainResidueDetails
BTHR35
BTHR46
DTHR35
DTHR46

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62328
ChainResidueDetails
BLYS38
BLYS44
BLYS51
DLYS38
DLYS44
DLYS51

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62328
ChainResidueDetails
BSER43
DSER43

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84
CLYS84

224572

PDB entries from 2024-09-04

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