MolNFT v1 · #125145 · protein

Human metavinculin (residues 959-1134) in complex with PIP2

5L0C: “Human metavinculin (residues 959-1134) in complex with PIP2”. X-ray diffraction, 2 ligands (PIO, PO4). MolNFT v1 #125145 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5L0C
Type: protein
Length: 692 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P18206
Ligands: PIO, PO4

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	176	—	P18206
B, C	—	protein	175	—	P18206
D	—	protein	166	—	P18206

Ligands and binding sites

PIO · [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2, 3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate · ligand · 5 copies · chains A, B, D, C
PO4 · Phosphate ion · ion · 3 copies · chains A, B

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

Compared structures

5L0C · Human metavinculin (residues 959-1134) in complex with PIP2 · the same entry in another collection · chain A against A, TM-score 1.00
P18206 · AlphaFold monomer V2.0 prediction for vinculin (P18206) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 P18206
Elsewhere: RCSB PDB 5L0C · PDBe 5L0C · UniProt P18206

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