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6DJO

Cryo-EM structure of ADP-actin filaments

Functional Information from GO Data
ChainGOidnamespacecontents
A0001725cellular_componentstress fiber
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0016787molecular_functionhydrolase activity
A0030240biological_processskeletal muscle thin filament assembly
A0048741biological_processskeletal muscle fiber development
B0001725cellular_componentstress fiber
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0016787molecular_functionhydrolase activity
B0030240biological_processskeletal muscle thin filament assembly
B0048741biological_processskeletal muscle fiber development
C0001725cellular_componentstress fiber
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0016787molecular_functionhydrolase activity
C0030240biological_processskeletal muscle thin filament assembly
C0048741biological_processskeletal muscle fiber development
D0001725cellular_componentstress fiber
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0016787molecular_functionhydrolase activity
D0030240biological_processskeletal muscle thin filament assembly
D0048741biological_processskeletal muscle fiber development
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue MG A 801
ChainResidue
AGLN137
AADP802

site_idAC2
Number of Residues15
Detailsbinding site for residue ADP A 802
ChainResidue
ALYS213
AGLU214
AGLY301
AGLY302
AMET305
ATYR306
ALYS336
AMG801
AGLY13
ASER14
AGLY15
ALEU16
ALYS18
AGLY156
AASP157

site_idAC3
Number of Residues2
Detailsbinding site for residue MG B 801
ChainResidue
BGLN137
BADP802

site_idAC4
Number of Residues15
Detailsbinding site for residue ADP B 802
ChainResidue
BGLY13
BSER14
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BLYS213
BGLU214
BGLY301
BGLY302
BMET305
BTYR306
BLYS336
BMG801

site_idAC5
Number of Residues1
Detailsbinding site for residue MG C 801
ChainResidue
CADP802

site_idAC6
Number of Residues15
Detailsbinding site for residue ADP C 802
ChainResidue
CGLY13
CSER14
CGLY15
CLEU16
CLYS18
CGLY156
CASP157
CLYS213
CGLU214
CGLY301
CGLY302
CMET305
CTYR306
CLYS336
CMG801

site_idAC7
Number of Residues1
Detailsbinding site for residue MG D 801
ChainResidue
DADP802

site_idAC8
Number of Residues15
Detailsbinding site for residue ADP D 802
ChainResidue
DGLY13
DSER14
DGLY15
DLEU16
DLYS18
DGLY156
DASP157
DLYS213
DGLU214
DGLY301
DGLY302
DMET305
DTYR306
DLYS336
DMG801

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 Residues4
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:456601
ChainResidueDetails
AASP1
BASP1
CASP1
DASP1

site_idSWS_FT_FI2
Number of Residues8
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET44
AMET47
BMET44
BMET47
CMET44
CMET47
DMET44
DMET47

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU
ChainResidueDetails
AHIC73
BHIC73
CHIC73
DHIC73

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84
BLYS84
CLYS84
DLYS84

226707

PDB entries from 2024-10-30

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