MolNFT v1 · #15374 · protein

C-des mutant K223A with gly covalenty linked to the plp-cofactor

1N2T · L-CYSTEINE/CYSTINE lyase C-des: “C-des mutant K223A with gly covalenty linked to the plp-cofactor”. X-ray diffraction, 3 ligands (PLP, GLY, K), 5 pockets (best druggability 0.81). MolNFT v1 #15374 on GenesisL1: 3D structure, binding…

PDB: 1N2T
Type: protein
Length: 770 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-CYSTEINE/CYSTINE lyase C-des
EC: 4.4.1.-
Ligands: PLP, GLY, K
Pockets: 5 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	L-CYSTEINE/CYSTINE lyase C-des (EC 4.4.1.-)	protein	385	41% helix, 18% strand	—

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
GLY · Glycine · ligand · 2 copies · chains A, B
K · Potassium 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, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	155	0.81	0.98	30	empty
2	642	0.75	0.81	63	PLP, GLY
3	682	0.75	0.80	68	PLP, GLY
4	51	0.52	0.88	16	empty
5	50	0.48	0.86	19	empty

Interfaces

1 interface between chains.

A–B · 3035 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

1N2T · C-DES Mutant K223A with GLY Covalenty Linked to the PLP-cofactor · 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 1N2T · PDBe 1N2T

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