MolNFT v1 · #101741 · protein

Crystal structure of 1-pyrroline-4-hydroxy-2-carboxylate deaminase from brucella melitensis with covalently bound substrate

4O0K · Dihydrodipicolinate synthetase: “Crystal structure of 1-pyrroline-4-hydroxy-2-carboxylate deaminase from brucella melitensis with covalently…”. X-ray diffraction, 2 pockets (best druggability 0.60). MolNFT v1 #101741 on GenesisL1…

PDB: 4O0K
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrodipicolinate synthetase
EC: 3.5.4.22
UniProt: C0RKH4
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrodipicolinate synthetase (EC 3.5.4.22)	protein	323	54% helix, 11% strand	C0RKH4

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	248	0.60	0.79	35	empty
2	50	0.29	0.76	15	empty

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

4O0K · Crystal structure of 1-pyrroline-4-hydroxy-2-carboxylate deaminase from Brucella… · 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 C0RKH4
Elsewhere: RCSB PDB 4O0K · PDBe 4O0K · UniProt C0RKH4

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