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Genetic incorporation of a metal-ion chelating amino acid into proteins as biophysical probe

Analyse Genetic incorporation of a metal-ion chelating amino acid into proteins as… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FCA
Type: protein
Length: 582 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine synthase
EC: 2.5.1.47
Ligands: ZN
Pockets: 5 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cysteine synthase (EC 2.5.1.47)	protein	291	46% helix, 17% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

5 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	467	0.72	0.81	64	empty
2	248	0.71	0.86	47	empty
3	145	0.49	0.79	20	empty
4	69	0.36	0.77	16	empty
5	55	0.29	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 1091 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

3FCA · Genetic Incorporation of a Metal-ion Chelating Amino Acid into proteins as biophysical… · 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 3FCA · PDBe 3FCA

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