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VVA2 (strip crystal form)

Analyse VVA2 (strip crystal form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PP6
Type: protein
Length: 962 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Volvatoxin A2
UniProt: Q6USC4
Pockets: 13 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Volvatoxin A2	protein	194	26% helix, 33% strand	Q6USC4
E	Volvatoxin A2	protein	186	27% helix, 31% strand	Q6USC4

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	816	0.77	0.81	91	empty
2	888	0.71	0.76	76	empty
3	290	0.62	0.80	36	empty
4	156	0.60	0.83	24	empty
5	73	0.53	0.85	19	empty

Interfaces

7 interfaces between chains.

A–C · 600 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 546 Å² buried · 11 hydrogen bonds · protein-protein
C–E · 456 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 445 Å² buried · 1 hydrogen bond · protein-protein
C–D · 266 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1PP6 · VVA2 (strip crystal form) · the same entry in another collection · chain E against E, 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 Q6USC4
Elsewhere: RCSB PDB 1PP6 · PDBe 1PP6 · UniProt Q6USC4

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