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6RSW

HFD domain of mouse CAP1 bound to the pointed end of G-actin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001725cellular_componentstress fiber
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0010628biological_processpositive regulation of gene expression
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030027cellular_componentlamellipodium
A0030041biological_processactin filament polymerization
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031013molecular_functiontroponin I binding
A0031432molecular_functiontitin binding
A0031941cellular_componentfilamentous actin
A0032036molecular_functionmyosin heavy chain binding
A0032432cellular_componentactin filament bundle
A0042802molecular_functionidentical protein binding
A0044297cellular_componentcell body
A0048306molecular_functioncalcium-dependent protein binding
A0048741biological_processskeletal muscle fiber development
A0051017biological_processactin filament bundle assembly
A0090131biological_processmesenchyme migration
A0098723cellular_componentskeletal muscle myofibril
A0140660molecular_functioncytoskeletal motor activator activity
B0003779molecular_functionactin binding
B0030837biological_processnegative regulation of actin filament polymerization
C0003779molecular_functionactin binding
C0007010biological_processcytoskeleton organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 401
ChainResidue
AADP402
AHOH530
AHOH532
AHOH555
AHOH575
AHOH605

site_idAC2
Number of Residues27
Detailsbinding site for residue ADP A 402
ChainResidue
ALEU16
ALYS18
AGLY156
AASP157
AGLY182
AARG183
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ALYS336
AMG401
AHOH513
AHOH532
AHOH542
AHOH555
AHOH569
AHOH605
AHOH616
AHOH656
AGLY13
ASER14
AGLY15

site_idAC3
Number of Residues10
Detailsbinding site for residue EPE A 403
ChainResidue
ATYR218
AGLU226
ATHR229
ALEU236
AARG254
APRO307
AHOH526
AHOH626
AHOH679
AHOH705

site_idAC4
Number of Residues6
Detailsbinding site for residue MG B 401
ChainResidue
AHOH564
AHOH658
AHOH699
BGLU296
BHOH578
BHOH580

site_idAC5
Number of Residues6
Detailsbinding site for residue EPE B 402
ChainResidue
BSER244
BHIS245
BGLU246
BASP306
BTYR309
BHOH507

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_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: N6-acetyllysine => ECO:0000250|UniProtKB:Q01518
ChainResidueDetails
CLYS80

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:18034455
ChainResidueDetails
BTYR309
AMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS61

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK
ChainResidueDetails
AHIC73

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177

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PDB entries from 2024-11-06

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