MolNFT v2 · #171077 · protein

Structure of the human CAK in complex with THZ1

6XD3: “Structure of the human CAK in complex with THZ1”. Electron microscopy at 3.3, 1 ligand (V0G). MolNFT v2 #171077 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6XD3
Type: protein
Length: 644 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.3
Source: Homo sapiens
UniProt: P51948, P51946, P50613
Ligands: V0G

Structure

electron microscopy · resolution 3.3 · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	—	protein	65	—	P51948
I	—	protein	281	—	P51946
J	—	protein	298	—	P50613

Ligands and binding sites

V0G · N-(3-{[5-chloro-4-(1H-indol-3-yl)pyrimidin-2-yl]amino}phenyl)-4-{[4-(dimethylamino) butanoyl]amino}benzamide · ligand · chains J

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

Compared structures

6XD3 · Structure of the human cak in complex with THZ1 · the same entry in another collection · chain H against H, TM-score 1.00
P51946 · AlphaFold monomer V2.0 prediction for cyclin-H (P51946) · a predicted model of the same protein · chain I against A, TM-score 0.99
P50613 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 7 (P50613) · a predicted model of the same protein · chain J 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 P51948
Every structure of UniProt P51946
Every structure of UniProt P50613
Elsewhere: RCSB PDB 6XD3 · PDBe 6XD3 · UniProt P51948 · UniProt P51946 · UniProt P50613

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