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Structure of a MAPK pathway complex

Analyse Structure of a MAPK pathway complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q0T
Type: protein
Length: 1,322 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P15056, Q02750, V9P4T4
Ligands: LCJ, AGS, MG

Structure

electron microscopy · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	280	—	P15056
B	—	protein	278	—	P15056
C	—	protein	306	—	Q02750
X, Y	—	protein	229	—	V9P4T4

Ligands and binding sites

LCJ · 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy) imidazo[1,5-a]pyridine-6-carboxamide · ligand · chains C
AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains C
MG · Magnesium ion · metal

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

Compared structures

6Q0T · Structure of a MAPK pathway complex · the same entry in another collection · chain B against B, TM-score 1.00
P15056 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase B-RAF (P15056) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P15056
Every structure of UniProt Q02750
Every structure of UniProt V9P4T4
Elsewhere: RCSB PDB 6Q0T · PDBe 6Q0T · UniProt P15056 · UniProt Q02750 · UniProt V9P4T4

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