MolNFT v1 · #119129 · protein

CRIFT52 N-terminal domain

5FMR · Intraflagellar transport protein component IFT52: “CRIFT52 N-terminal domain”. X-ray diffraction, 1 ligand (SO4), 8 pockets (best druggability 0.64). MolNFT v1 #119129 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5FMR
Type: protein
Length: 728 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Intraflagellar transport protein component IFT52
UniProt: Q944U2
Ligands: SO4
Pockets: 8 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Intraflagellar transport protein component IFT52	protein	242	26% helix, 24% strand	Q944U2
C	Intraflagellar transport protein component IFT52	protein	244	25% helix, 24% strand	Q944U2

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B, C

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

Pockets

8 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	714	0.64	0.73	75	empty
2	103	0.35	0.73	22	empty
3	76	0.34	0.75	14	SO4
4	80	0.34	0.75	17	SO4
5	77	0.34	0.75	13	SO4

Interfaces

3 interfaces between chains.

B–C · 688 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 679 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 677 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5FMR · crIFT52 N-terminal domain · 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 Q944U2
Elsewhere: RCSB PDB 5FMR · PDBe 5FMR · UniProt Q944U2

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