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1MA9

Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin

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
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 Residues5
DetailsBINDING SITE FOR RESIDUE MG B 376
ChainResidue
BATP377
BHOH415
BHOH493
BHOH494
BHOH495

site_idAC2
Number of Residues30
DetailsBINDING SITE FOR RESIDUE ATP B 377
ChainResidue
BLYS18
BGLY156
BASP157
BGLY158
BVAL159
BGLY182
BARG210
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BTYR306
BLYS336
BMG376
BHOH384
BHOH393
BHOH399
BHOH415
BHOH422
BHOH441
BHOH475
BHOH493
BHOH494
BHOH495
BGLY13
BSER14
BGLY15
BLEU16

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
BTHR6

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
BGLN49
BSER52

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
BTHR66

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
BASN78

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
BTHR89

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
BGLY182

224004

PDB entries from 2024-08-21

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