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6QRI

Structure of rabbit G-actin in complex with chivosazole A

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
B0000287molecular_functionmagnesium ion binding
B0001725cellular_componentstress fiber
B0003785molecular_functionactin monomer binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005523molecular_functiontropomyosin binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0010628biological_processpositive regulation of gene expression
B0016787molecular_functionhydrolase activity
B0019904molecular_functionprotein domain specific binding
B0030027cellular_componentlamellipodium
B0030041biological_processactin filament polymerization
B0030175cellular_componentfilopodium
B0030240biological_processskeletal muscle thin filament assembly
B0031013molecular_functiontroponin I binding
B0031432molecular_functiontitin binding
B0031941cellular_componentfilamentous actin
B0032036molecular_functionmyosin heavy chain binding
B0032432cellular_componentactin filament bundle
B0042802molecular_functionidentical protein binding
B0044297cellular_componentcell body
B0048306molecular_functioncalcium-dependent protein binding
B0048741biological_processskeletal muscle fiber development
B0051017biological_processactin filament bundle assembly
B0090131biological_processmesenchyme migration
B0098723cellular_componentskeletal muscle myofibril
B0140660molecular_functioncytoskeletal motor activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue ATP B 401
ChainResidue
BGLY13
BGLY182
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BLYS336
BMG402
BHOH502
BSER14
BHOH503
BHOH505
BHOH511
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BGLY158
BVAL159

site_idAC2
Number of Residues5
Detailsbinding site for residue MG B 402
ChainResidue
BATP401
BHOH501
BHOH502
BHOH505
BHOH511

site_idAC3
Number of Residues15
Detailsbinding site for residue CV9 B 403
ChainResidue
ASER145
AGLY146
AARG147
ALYS328
ACV9403
BGLY23
BASP24
BASP25
BTYR143
BALA144
BGLY146
BILE341
BSER344
BILE345
BLEU349

site_idAC4
Number of Residues25
Detailsbinding site for residue ATP A 401
ChainResidue
AGLY13
ASER14
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ALYS336
AMG402
AHOH502
AHOH509
AHOH510
AHOH517
AHOH518

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
AATP401
AHOH508
AHOH510
AHOH513
AHOH516
AHOH518

site_idAC6
Number of Residues16
Detailsbinding site for residue CV9 A 403
ChainResidue
AASP24
AASP25
ATYR143
AALA144
AGLY146
AGLU334
AILE341
ASER344
AILE345
ALEU349
ATHR351
AHOH524
BSER145
BARG147
BILE330
BCV9403

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
BTYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
BTRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
BLEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737
ChainResidueDetails
BCYS0
ACYS0

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665
ChainResidueDetails
BASP1
AASP1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
BMET44
BMET47
AMET44
AMET47

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
BLYS61
ALYS61

site_idSWS_FT_FI5
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
BHIC73
AHIC73

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
BLYS84
ALYS84

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
BARG177
AARG177

223532

PDB entries from 2024-08-07

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