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MMIFT54 ch-domain

Analyse MMIFT54 ch-domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FMU
Type: protein
Length: 528 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRAF3-interacting protein 1
UniProt: Q149C2
Pockets: 5 · best druggability 0.69

Structure

x-ray diffraction · 4 distinct chains · 63% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRAF3-interacting protein 1	protein	131	64% helix, 0% strand	Q149C2
B	TRAF3-interacting protein 1	protein	132	61% helix, 0% strand	Q149C2
C	TRAF3-interacting protein 1	protein	132	63% helix, 0% strand	Q149C2
D	TRAF3-interacting protein 1	protein	133	62% helix, 0% strand	Q149C2

Ligands and binding sites

MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains B, C

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	564	0.69	0.78	84	empty
2	226	0.66	0.83	30	empty
3	251	0.65	0.83	32	MES
4	269	0.58	0.79	32	empty
5	98	0.42	0.78	20	empty

Interfaces

5 interfaces between chains.

B–D · 492 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 473 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 379 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 359 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 280 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5FMU · MmIFT54 CH-domain · the same entry in another collection · chain D against D, TM-score 1.00
Q149C2 · AlphaFold monomer V2.0 prediction for TRAF3-interacting protein 1 (Q149C2) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q149C2
Elsewhere: RCSB PDB 5FMU · PDBe 5FMU · UniProt Q149C2

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