MolNFT v1 · #116633 · protein

Crystal structure of the CC1-fha tandem of kinesin-3 KIF13A

5DJO · Kinesin-like protein: “Crystal structure of the CC1-fha tandem of kinesin-3 KIF13A”. X-ray diffraction, 2 pockets (best druggability 0.58). MolNFT v1 #116633 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5DJO
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin-like protein
UniProt: F8VQ75
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin-like protein	protein	158	27% helix, 31% strand	F8VQ75
B	Kinesin-like protein	protein	160	26% helix, 32% strand	F8VQ75

Ligands and binding sites

FMT · Formic acid · additive · 5 copies · chains A, B
ACY · Acetic acid · additive · chains B
PEG · Di(hydroxyethyl)ether · additive · chains B

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.58	0.84	26	empty
2	76	0.32	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 2228 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

5DJO · Crystal structure of the CC1-FHA tandem of Kinesin-3 KIF13A · the same entry in another collection · chain A against A, TM-score 1.00

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 F8VQ75
Elsewhere: RCSB PDB 5DJO · PDBe 5DJO · UniProt F8VQ75

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