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1LOT

CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING PROTEIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0005499molecular_functionvitamin D binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0035461biological_processvitamin transmembrane transport
A0042359biological_processvitamin D metabolic process
A0043202cellular_componentlysosomal lumen
A0051180biological_processvitamin transport
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0090482molecular_functionvitamin transmembrane transporter activity
A1902118molecular_functioncalcidiol binding
B0000166molecular_functionnucleotide binding
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 CA B 550
ChainResidue
BATP500
BHOH652
BHOH653
BHOH655
BHOH658
BHOH666

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ATP B 500
ChainResidue
BLEU16
BLYS18
BGLY156
BASP157
BGLY158
BVAL159
BGLY182
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BTYR306
BLYS336
BCA550
BHOH651
BHOH653
BHOH655
BHOH661
BHOH666
BHOH693
BGLY13
BSER14
BGLY15

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 600
ChainResidue
AGLU186
AGLN189
BGLU241

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 610
ChainResidue
AASP309
AILE384
AASP385

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 620
ChainResidue
AARG133
BVAL30
BASP56
BGLU93

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 630
ChainResidue
ATYR394
AASN397
ATHR398
APHE399
BASN280
BMET283
BLYS284
BHOH685

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 640
ChainResidue
BASP179
BASP184
BMET269

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 650
ChainResidue
BGLY23
BASP25
BHOH687

Functional Information from PROSITE/UniProt
site_idPS00212
Number of Residues25
DetailsALBUMIN_1 Albumin domain signature. YlsmvgsCCtsAsptvCFlkerlqL
ChainResidueDetails
ATYR166-LEU190

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 Residues1
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665
ChainResidueDetails
BASP1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
BMET44
BMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
BLYS61

site_idSWS_FT_FI4
Number of Residues1
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

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
BLYS84

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
BARG177

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PDB entries from 2024-04-24

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