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2VYP

Rabbit-muscle G-actin in complex with myxobacterial rhizopodin

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 Residues27
DetailsBINDING SITE FOR RESIDUE ATP A1375
ChainResidue
AGLY13
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ALYS336
ASER14
ACA1376
AHOH2002
AHOH2063
AHOH2098
AHOH2137
AHOH2138
AHOH2139
AHOH2140
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A1376
ChainResidue
AATP1375
AHOH2002
AHOH2003
AHOH2038
AHOH2140

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B1376
ChainResidue
AGLU167
BGLN354
BTRP356
BGLU361

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATP B1377
ChainResidue
BGLY13
BSER14
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BGLY158
BVAL159
BGLY182
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BTYR306
BCA1378
BHOH2021
BHOH2022
BHOH2061
BHOH2062

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B1378
ChainResidue
BATP1377
BHOH2002
BHOH2016
BHOH2021
BHOH2062

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B1379
ChainResidue
BASP286
BASP288

site_idAC7
Number of Residues32
DetailsBINDING SITE FOR RESIDUE RH9 A1377
ChainResidue
ATYR133
ATYR143
AALA144
ASER145
AGLY146
AARG147
ATHR148
AGLY168
ATYR169
AILE345
ALEU346
ALEU349
AHEZ1378
AHOH2141
AHOH2142
AHOH2143
AHOH2144
AHOH2145
AHOH2146
AHOH2147
AHOH2148
BTYR143
BALA144
BSER145
BGLY146
BARG147
BGLY168
BTYR169
BILE345
BLEU346
BTHR351
BHOH2015

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HEZ A1378
ChainResidue
ARH91377
AHOH2129
AHOH2151
BGLU167
BTYR169
BPHE375
ALEU349
ATHR351

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HEZ A1379
ChainResidue
AASP24
AASP25
AALA26
APRO27

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HEZ A1380
ChainResidue
APRO27
AHOH2152
AHOH2153

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-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737
ChainResidueDetails
ACYS0
BCYS0

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

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

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

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
AHIS73
BHIS73

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

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

221051

PDB entries from 2024-06-12

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