Research workbench

Apo HA17-HA33

Analyse Apo HA17-HA33 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LO0
Type: protein
Length: 715 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ha-33; Ha-17
UniProt: Q45871, Q45878
Pockets: 7 · best druggability 0.49

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ha-33	protein	286	10% helix, 48% strand	Q45871
C	Ha-17	protein	144	6% helix, 51% strand	Q45878
B	Ha-33	protein	285	8% helix, 47% strand	Q45871

Pockets

7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	156	0.49	0.78	23	empty
2	123	0.44	0.77	23	empty
3	107	0.43	0.77	23	empty
4	126	0.38	0.73	17	empty
5	51	0.34	0.78	12	empty

Interfaces

3 interfaces between chains.

A–B · 982 Å² buried · 14 hydrogen bonds · protein-protein
C–B · 707 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 452 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4LO0 · Apo HA17-HA33 · 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 Q45871
Every structure of UniProt Q45878
Elsewhere: RCSB PDB 4LO0 · PDBe 4LO0 · UniProt Q45871 · UniProt Q45878

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