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CU(II) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia COLI

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

PDB: 6KYY
Type: protein
Length: 1,753 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyridine nucleotide-disulphide oxidoreductase dimerisation region
UniProt: A0A140ND83
Ligands: FAD, CU, CL
Pockets: 12 · best druggability 0.85

Structure

x-ray diffraction · 3 distinct chains · 33% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyridine nucleotide-disulphide oxidoreductase dimerisation region	protein	432	33% helix, 23% strand	A0A140ND83
B, C	Pyridine nucleotide-disulphide oxidoreductase dimerisation region	protein	441	34% helix, 24% strand	A0A140ND83
D	Pyridine nucleotide-disulphide oxidoreductase dimerisation region	protein	439	31% helix, 23% strand	A0A140ND83

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
CU · Copper (II) ion · metal · 32 copies · chains A, B, C, D
CL · Chloride ion · ion · 2 copies · chains B, C

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

Pockets

12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1198	0.85	0.86	137	FAD, CL
2	1011	0.81	0.82	106	FAD
3	827	0.79	0.82	96	FAD, CL
4	456	0.78	0.86	49	CU
5	741	0.78	0.82	88	FAD

Interfaces

3 interfaces between chains.

C–D · 2374 Å² buried · 29 hydrogen bonds · protein-protein
A–B · 2349 Å² buried · 28 hydrogen bonds · protein-protein
B–C · 851 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6KYY · Cu(II) complex of HOCl-induced flavoprotein disulfide reductase RclA from Escherichia coli · 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 6KYY · PDBe 6KYY · UniProt A0A140ND83

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