MolNFT v1 · #27381 · protein

Clathrin D6 coat

1XI4 · Clathrin heavy chain: “Clathrin D6 coat”. Electron microscopy, 20 pockets (best druggability 0.67). MolNFT v1 #27381 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1XI4
Type: protein
Length: 15,300 residues
Chains: 18
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Clathrin heavy chain; Clathrin light chain a
UniProt: P49951, P04973
Pockets: 20 · best druggability 0.67

Structure

electron microscopy · 2 distinct chains · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I	Clathrin heavy chain	protein	1630	0% helix, 0% strand	P49951
J, K, L, M, N, O, P, Q, R	Clathrin light chain a	protein	70	0% helix, 0% strand	P04973

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	600	0.67	0.75	94	empty
2	514	0.65	0.75	78	empty
3	424	0.62	0.74	69	empty
4	344	0.57	0.73	54	empty
5	256	0.53	0.74	50	empty

Interfaces

25 interfaces between chains.

F–G · 567 Å² buried · 0 hydrogen bonds · protein-protein
C–D · 391 Å² buried · 0 hydrogen bonds · protein-protein
A–F · 320 Å² buried · 0 hydrogen bonds · protein-protein
E–H · 244 Å² buried · 0 hydrogen bonds · protein-protein
G–I · 129 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1XI4 · Clathrin D6 Coat · the same entry in another collection · chain N against N, 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 P49951
Every structure of UniProt P04973
Elsewhere: RCSB PDB 1XI4 · PDBe 1XI4 · UniProt P49951 · UniProt P04973

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