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Clathrin heavy-chain terminal domain and linker

Analyse Clathrin heavy-chain terminal domain and linker in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BPO
Type: protein
Length: 1,467 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (clathrin)
UniProt: P11442
Pockets: 15 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Protein (clathrin)	protein	487	23% helix, 36% strand	P11442
B	Protein (clathrin)	protein	493	23% helix, 36% strand	P11442

Pockets

15 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	1105	0.86	0.87	115	empty
2	795	0.78	0.82	73	empty
3	739	0.77	0.82	70	empty
4	456	0.58	0.74	51	empty
5	224	0.49	0.75	32	empty

Interfaces

2 interfaces between chains.

B–C · 1077 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 840 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1BPO · Clathrin heavy-chain terminal domain and linker · the same entry in another collection · chain A against A, TM-score 1.00
P11442 · AlphaFold monomer V2.0 prediction for clathrin heavy chain 1 (P11442) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P11442
Elsewhere: RCSB PDB 1BPO · PDBe 1BPO · UniProt P11442

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