MolNFT v1 · #129586 · protein

Structure of CHK1 10-pt. mutant complex with AMP-pnp

5OOP: “Structure of CHK1 10-pt. mutant complex with AMP-pnp”. X-ray diffraction, 1 ligand (ANP). MolNFT v1 #129586 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5OOP
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O14757
Ligands: ANP

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	261	—	O14757

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A

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

Compared structures

5OOP · Structure of CHK1 10-pt. mutant complex with AMP-PNP · the same entry in another collection · chain A against A, TM-score 1.00
O14757 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase CHK1 (O14757) · a predicted model of the same protein · chain A against A, TM-score 0.98
2C3K · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain A against A, TM-score 0.98
2C3L · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain A against A, TM-score 0.97
2C3J · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain A 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 O14757
Elsewhere: RCSB PDB 5OOP · PDBe 5OOP · UniProt O14757

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