Research workbench

Crystal structure of the zn-directed tetramer of the engineered cyt cb 562 variant, C96I/A38S AB5

Analyse Crystal structure of the zn-directed tetramer of the engineered cyt cb 562… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DCL
Type: protein
Length: 212 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Engineered cyt cb 562 variant, AB5
Ligands: HEC, ZN, CL
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Engineered cyt cb 562 variant, AB5	protein	106	79% helix, 0% strand	—

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 8 copies · chains A, B
CL · Chloride ion · ion · chains A

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

Pockets

2 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	132	0.60	0.84	23	HEC
2	159	0.58	0.82	24	HEC

Interfaces

1 interface between chains.

A–B · 813 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

Compared structures

7DCL · Crystal structure of the Zn-directed tetramer of the engineered cyt cb 562 variant… · 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
Elsewhere: RCSB PDB 7DCL · PDBe 7DCL

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