Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2HMP

Uncomplexed actin cleaved with protease ECP32

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 Residues6
DetailsBINDING SITE FOR RESIDUE SR A 1391
ChainResidue
AATP5381
AHOH6604
AHOH6607
AHOH6608
AHOH6609
AHOH6610

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SR B 1392
ChainResidue
BHOH6626
BHOH6627
BHOH6640
BATP5382
BHOH6607
BHOH6619

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SR A 2001
ChainResidue
AGLU125
AASN128
AHOH6910
AHOH6945
AHOH6951
AHOH6952

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SR A 2002
ChainResidue
AHOH6793
AHOH6816
AHOH6822
AHOH6837
AHOH6885
AHOH6896
AHOH6917

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SR B 2003
ChainResidue
AASP363
BGLU125
BASN128
BHOH6647
BHOH6715
BHOH6719
BHOH6759
BHOH6807

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SR B 2004
ChainResidue
BVAL30
BHOH6675
BHOH6685
BHOH6766
BHOH6793

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SR B 2005
ChainResidue
AHOH6839
AHOH6855
BHOH6711
BHOH6824
BHOH6825

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SPD A 5400
ChainResidue
ASER145
AGLY146
AARG147
AASN296
BGLN353
BGLN354

site_idAC9
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ATP A 5381
ChainResidue
AGLY13
ASER14
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159
AGLY182
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ASR1391
AHOH6604
AHOH6608
AHOH6612
AHOH6617
AHOH6629
AHOH6657
AHOH6738
AHOH6751

site_idBC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ATP B 5382
ChainResidue
BHOH6646
BHOH6728
BHOH6743
BGLY13
BSER14
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BGLY158
BVAL159
BGLY182
BARG210
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BTYR306
BLYS336
BSR1392
BHOH6604
BHOH6607
BHOH6626
BHOH6645

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 5500
ChainResidue
AALA310
AGLN314
AILE329

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 5501
ChainResidue
AGLY23
AASP24
AASP25
ASER344
AHOH6948

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 5502
ChainResidue
ATYR188
AARG256
APHE266
AEDO5503
AHOH6757
BALA231

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 5503
ChainResidue
AGLU195
AARG256
AEDO5502
AHOH6723
AHOH6753
BARG196
BALA230
BASN252

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 5504
ChainResidue
ATYR198
ASER199
APHE200
AHOH6746

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 5505
ChainResidue
BGLY23
BASP24
BASP25
BSER344
BHOH6790

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 5506
ChainResidue
AALA29
AVAL30
AHOH6766

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 5507
ChainResidue
BALA144
BSER145
BPRO332
BGLU334
BSER338
BHOH6620
BHOH6763
BHOH6809

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 5508
ChainResidue
AALA135
AILE136
AVAL139
ATYR143
APHE375

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 211 B 6600
ChainResidue
ATHR351
BTYR143
BTHR148
BGLU167

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 211 A 6601
ChainResidue
ATHR148
AGLU167
BTHR351

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
BASP1

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET44
AMET47
BMET44
BMET47

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS61
BLYS61

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
BHIC73

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84
BLYS84

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177
BARG177

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon