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7C2F

Crystal Structure of the Thorarchaeota ProGel/rabbit actin complex

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
C0000287molecular_functionmagnesium ion binding
C0001725cellular_componentstress fiber
C0003785molecular_functionactin monomer binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005523molecular_functiontropomyosin binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0010628biological_processpositive regulation of gene expression
C0016787molecular_functionhydrolase activity
C0019904molecular_functionprotein domain specific binding
C0030027cellular_componentlamellipodium
C0030041biological_processactin filament polymerization
C0030175cellular_componentfilopodium
C0030240biological_processskeletal muscle thin filament assembly
C0031013molecular_functiontroponin I binding
C0031432molecular_functiontitin binding
C0031941cellular_componentfilamentous actin
C0032036molecular_functionmyosin heavy chain binding
C0032432cellular_componentactin filament bundle
C0042802molecular_functionidentical protein binding
C0044297cellular_componentcell body
C0048306molecular_functioncalcium-dependent protein binding
C0048741biological_processskeletal muscle fiber development
C0051017biological_processactin filament bundle assembly
C0090131biological_processmesenchyme migration
C0098723cellular_componentskeletal muscle myofibril
C0140660molecular_functioncytoskeletal motor activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue LAB A 401
ChainResidue
AGLY15
ATHR186
AARG206
AGLU207
AARG210
ALYS213
AHOH632
ALEU16
APRO32
AILE34
AGLN59
ATYR69
AASP157
AGLY182
AARG183

site_idAC2
Number of Residues31
Detailsbinding site for residue ATP A 402
ChainResidue
AGLY13
ASER14
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ALYS336
AMG403
AHOH526
AHOH554
AHOH565
AHOH580
AHOH583
AHOH586
AHOH599
AHOH605
AHOH613
AHOH673
AHOH694

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 403
ChainResidue
AATP402
AHOH554
AHOH565
AHOH599
AHOH673

site_idAC4
Number of Residues15
Detailsbinding site for residue LAB C 401
ChainResidue
CGLY15
CLEU16
CILE34
CGLN59
CARG62
CTYR69
CASP157
CGLY182
CARG183
CTHR186
CARG206
CGLU207
CARG210
CLYS213
CHOH623

site_idAC5
Number of Residues31
Detailsbinding site for residue ATP C 402
ChainResidue
CGLY13
CSER14
CGLY15
CLEU16
CLYS18
CGLY156
CASP157
CGLY158
CVAL159
CGLY182
CARG210
CLYS213
CGLU214
CGLY301
CGLY302
CTHR303
CMET305
CTYR306
CLYS336
CMG403
CHOH530
CHOH531
CHOH545
CHOH555
CHOH562
CHOH571
CHOH583
CHOH586
CHOH612
CHOH624
CHOH661

site_idAC6
Number of Residues5
Detailsbinding site for residue MG C 403
ChainResidue
CHOH531
CHOH555
CHOH624
CATP402
CHOH530

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 Residues2
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665
ChainResidueDetails
AASP1
CASP1

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET44
AMET47
CMET44
CMET47

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS61
CLYS61

site_idSWS_FT_FI4
Number of Residues2
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
CHIC73

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84
CLYS84

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177
CARG177

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PDB entries from 2024-07-24

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