MolNFT v1 · #147594 · protein

Cytosolic copper storage protein csp from streptomyces lividans: apo form

6EI0 · Cytosolic copper storage protein (ccsp): “Cytosolic copper storage protein csp from streptomyces lividans: apo form”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.85). MolNFT v1 #147594 on GenesisL1: 3D…

PDB: 6EI0
Type: protein
Length: 468 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytosolic copper storage protein (ccsp)
UniProt: A0A1H2BDT0
Ligands: SO4
Pockets: 3 · best druggability 0.85

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
Q	Cytosolic copper storage protein (ccsp)	protein	119	84% helix, 0% strand	A0A1H2BDT0
G, U	Cytosolic copper storage protein (ccsp)	protein	116	85% helix, 0% strand	A0A1H2BDT0
N	Cytosolic copper storage protein (ccsp)	protein	117	85% helix, 0% strand	A0A1H2BDT0

Ligands and binding sites

SO4 · Sulfate ion · ion · chains Q, U, N
GOL · Glycerol · additive · chains G
PGE · Triethylene glycol · additive · chains G

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

Pockets

3 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	350	0.85	0.94	71	empty
2	88	0.38	0.76	18	empty
3	78	0.35	0.76	13	empty

Interfaces

6 interfaces between chains.

Q–N · 1063 Å² buried · 12 hydrogen bonds · protein-protein
G–U · 1028 Å² buried · 13 hydrogen bonds · protein-protein
Q–G · 726 Å² buried · 11 hydrogen bonds · protein-protein
U–N · 716 Å² buried · 11 hydrogen bonds · protein-protein
Q–U · 431 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6EI0 · Cytosolic copper storage protein Csp from Streptomyces lividans: apo form · the same entry in another collection · chain Q against Q, 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 A0A1H2BDT0
Elsewhere: RCSB PDB 6EI0 · PDBe 6EI0 · UniProt A0A1H2BDT0

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