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Apo-CSP1 (copper storage protein 1) from methylosinus trichosporium OB3B

Analyse Apo-CSP1 (copper storage protein 1) from methylosinus trichosporium OB3B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FJD
Type: protein
Length: 442 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Copper storage protein 1
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Copper storage protein 1	protein	110	79% helix, 0% strand	—
B, D	Copper storage protein 1	protein	111	78% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	323	0.84	0.94	50	empty
2	65	0.31	0.75	20	empty

Interfaces

6 interfaces between chains.

C–D · 868 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 861 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 847 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 826 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 561 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5FJD · Apo-CSP1 (copper storage protein 1) from methylosinus trichosporium OB3B · 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 5FJD · PDBe 5FJD

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