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Structure of ARHGAP12 bound to G-actin

Analyse Structure of ARHGAP12 bound to G-actin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GVC
Type: protein
Length: 2,308 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P68135, Q8C0D4
Ligands: LAB, ATP, MG

Structure

x-ray diffraction · 7 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, C	—	protein	359	—	P68135
A	—	protein	356	—	P68135
D	—	protein	356	—	P68135
R	—	protein	216	—	Q8C0D4
Q	—	protein	223	—	Q8C0D4
S	—	protein	217	—	Q8C0D4
T	—	protein	222	—	Q8C0D4

Ligands and binding sites

LAB · Latrunculin B · ligand · 4 copies · chains B, A, C, D
ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains B, A, C, D
MG · Magnesium ion · metal · 4 copies · chains B, C, D
EDO · 1,2-ethanediol · additive · 8 copies · chains B, R, A, S, C, T, D, Q

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6GVC · Structure of ArhGAP12 bound to G-Actin · the same entry in another collection · chain T against T, TM-score 1.00
P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain D against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P68135
Every structure of UniProt Q8C0D4
Elsewhere: RCSB PDB 6GVC · PDBe 6GVC · UniProt P68135 · UniProt Q8C0D4

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