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4RWT

Structure of actin-Lmod complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000281biological_processmitotic cytokinesis
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0006338biological_processchromatin remodeling
A0007291biological_processsperm individualization
A0016787molecular_functionhydrolase activity
A0030723biological_processovarian fusome organization
A0031011cellular_componentIno80 complex
A0032507biological_processmaintenance of protein location in cell
A0035060cellular_componentbrahma complex
A0035148biological_processtube formation
B0000281biological_processmitotic cytokinesis
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0006338biological_processchromatin remodeling
B0007291biological_processsperm individualization
B0016787molecular_functionhydrolase activity
B0030723biological_processovarian fusome organization
B0031011cellular_componentIno80 complex
B0032507biological_processmaintenance of protein location in cell
B0035060cellular_componentbrahma complex
B0035148biological_processtube formation
C0003779molecular_functionactin binding
C0003785molecular_functionactin monomer binding
C0005523molecular_functiontropomyosin binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0006936biological_processmuscle contraction
C0007015biological_processactin filament organization
C0030016cellular_componentmyofibril
C0030017cellular_componentsarcomere
C0030041biological_processactin filament polymerization
C0030239biological_processmyofibril assembly
C0030838biological_processpositive regulation of actin filament polymerization
C0031430cellular_componentM band
C0045010biological_processactin nucleation
C0045214biological_processsarcomere organization
C0051694biological_processpointed-end actin filament capping
D0003779molecular_functionactin binding
D0003785molecular_functionactin monomer binding
D0005523molecular_functiontropomyosin binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0006936biological_processmuscle contraction
D0007015biological_processactin filament organization
D0030016cellular_componentmyofibril
D0030017cellular_componentsarcomere
D0030041biological_processactin filament polymerization
D0030239biological_processmyofibril assembly
D0030838biological_processpositive regulation of actin filament polymerization
D0031430cellular_componentM band
D0045010biological_processactin nucleation
D0045214biological_processsarcomere organization
D0051694biological_processpointed-end actin filament capping
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ANP A 401
ChainResidue
AGLY13
ALYS213
AGLU214
AGLY302
AMET305
ATYR306
ALYS336
AMG402
ASER14
AGLY15
AMET16
ALYS18
AGLY156
AASP157
AGLY182
AARG210

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AGLN137
AANP401

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ANP B 401
ChainResidue
BGLY13
BSER14
BGLY15
BMET16
BLYS18
BGLY156
BASP157
BGLY182
BARG210
BLYS213
BGLU214
BGLY302
BTHR303
BMET305
BTYR306
BMG402

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BGLN137
BANP401

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. WISKqEYDE
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: Phosphoserine => ECO:0000250|UniProtKB:Q3UHZ5
ChainResidueDetails
CSER11
CSER15
DSER11
DSER15

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:A1A5Q0
ChainResidueDetails
CSER24
CLYS400
DSER24
DLYS400

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Tele-methylhistidine => ECO:0000250|UniProtKB:P02572
ChainResidueDetails
AHIS73
BHIS73

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PDB entries from 2024-11-06

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