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Structure of the artificial complex alpha-REP/OCTARELLIN V.1 crystallized by counter diffusion in a capillary

Analyse Structure of the artificial complex alpha-REP/OCTARELLIN V.1 crystallized by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BZX
Type: protein
Length: 475 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-rep; Octarellin V.1
Ligands: NA
Pockets: 5 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-rep	protein	280	76% helix, 0% strand	—
B	Octarellin V.1	protein	195	39% helix, 13% strand	—

Ligands and binding sites

NA · Sodium ion · metal · chains B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	330	0.83	0.92	42	NA
2	128	0.64	0.87	26	empty
3	151	0.46	0.76	19	empty
4	108	0.44	0.79	19	empty
5	82	0.36	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 1771 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

6BZX · Structure of the artificial complex alpha-Rep/Octarellin V.1 crystallized by counter… · 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
Elsewhere: RCSB PDB 6BZX · PDBe 6BZX

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