MolNFT v1 · #161151 · protein

Copper loading to a cytosolic copper storage protein from streptomyces lividans (five coppers)

6Q58: “Copper loading to a cytosolic copper storage protein from streptomyces lividans (five coppers)”. X-ray diffraction, 1 ligand (CU1), 6 pockets (best druggability 0.57). MolNFT v1 #161151 on GenesisL1: 3D structure, binding sites and…

PDB: 6Q58
Type: protein
Length: 471 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytosolic copper storage protein
UniProt: Q9X8F4
Ligands: CU1
Pockets: 6 · best druggability 0.57

Structure

x-ray diffraction · 3 distinct chains · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, C	Cytosolic copper storage protein	protein	117	85% helix, 0% strand	Q9X8F4
D	Cytosolic copper storage protein	protein	117	86% helix, 0% strand	Q9X8F4
A	Cytosolic copper storage protein	protein	120	84% helix, 0% strand	Q9X8F4

Ligands and binding sites

CU1 · Copper (I) ion · metal · 15 copies · chains B, C, D, A

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

Pockets

6 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	192	0.57	0.80	38	empty
2	84	0.56	0.86	15	empty
3	103	0.40	0.77	19	empty
4	124	0.40	0.75	21	empty
5	77	0.37	0.77	18	empty

Interfaces

5 interfaces between chains.

B–C · 1062 Å² buried · 14 hydrogen bonds · protein-protein
B–A · 716 Å² buried · 13 hydrogen bonds · protein-protein
B–D · 526 Å² buried · 10 hydrogen bonds · protein-protein
C–A · 428 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 270 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6Q58 · Copper loading to a cytosolic copper storage protein from Streptomyces lividans (five… · the same entry in another collection · chain B against B, 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 Q9X8F4
Elsewhere: RCSB PDB 6Q58 · PDBe 6Q58 · UniProt Q9X8F4

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