Research workbench

Copper transporter oprc

Analyse Copper transporter oprc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Z99
Type: protein
Length: 1,312 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative copper transport outer membrane porin oprc
UniProt: G3XD89
Ligands: AG
Pockets: 19 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative copper transport outer membrane porin oprc	protein	654	5% helix, 57% strand	G3XD89
B	Putative copper transport outer membrane porin oprc	protein	658	5% helix, 55% strand	G3XD89

Ligands and binding sites

AG · Silver ion · metal · 6 copies · chains A, B

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

Pockets

19 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	243	0.84	0.96	44	empty
2	262	0.84	0.95	47	empty
3	276	0.84	0.95	52	empty
4	169	0.81	0.96	41	empty
5	1142	0.80	0.81	79	AG

Interfaces

1 interface between chains.

A–B · 616 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

6Z99 · Copper transporter OprC · 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
Every structure of UniProt G3XD89
Elsewhere: RCSB PDB 6Z99 · PDBe 6Z99 · UniProt G3XD89

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.