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Cu(II) complex of HOCl-induced flavoprotein disulfide reductase RclA C43S mutant from Escherichia coli

Analyse Cu(II) complex of HOCl-induced flavoprotein disulfide reductase RclA C43S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KOD
Type: protein
Length: 1,763 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3
Source: Escherichia coli BL21(DE3)
Molecule: Pyridine nucleotide-disulphide oxidoreductase dimerisation region
UniProt: A0A140ND83
Ligands: FAD, CU, CL
Pockets: 15 · best druggability 0.82

Structure

x-ray diffraction · resolution 3 · 2 distinct chains · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyridine nucleotide-disulphide oxidoreductase dimerisation region	protein	440	34% helix, 25% strand	A0A140ND83
B, C, D	Pyridine nucleotide-disulphide oxidoreductase dimerisation region	protein	441	33% helix, 26% strand	A0A140ND83

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
CU · Copper (II) ion · metal · 52 copies · chains A, B, C, D
CL · Chloride ion · ion · chains B

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

Pockets

15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1053	0.82	0.83	120	FAD, CL, CU
2	742	0.79	0.83	86	FAD, CU
3	683	0.77	0.82	81	FAD
4	619	0.77	0.83	73	FAD
5	404	0.75	0.85	48	CU

Interfaces

3 interfaces between chains.

C–D · 2420 Å² buried · 32 hydrogen bonds · protein-protein
A–B · 2411 Å² buried · 29 hydrogen bonds · protein-protein
B–C · 879 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6KOD · CU(II) complex of hocl-induced flavoprotein disulfide reductase rcla C43S mutant from… · 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 A0A140ND83
Elsewhere: RCSB PDB 6KOD · PDBe 6KOD · UniProt A0A140ND83

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