MolNFT v1 · #101503 · protein

Crystal structure of hlmi

4NTD · Thioredoxin reductase: “Crystal structure of hlmi”. X-ray diffraction, 4 ligands (GSH, FAD, CL), 3 pockets (best druggability 0.77). MolNFT v1 #101503 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4NTD
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin reductase
UniProt: E2PZ87
Ligands: GSH, FAD, CL, PO4
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin reductase	protein	318	31% helix, 26% strand	E2PZ87

Ligands and binding sites

GSH · Glutathione · ligand · chains A
FAD · Flavin-adenine dinucleotide · ligand · chains A
CL · Chloride ion · ion · chains A
PO4 · Phosphate ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Pockets

3 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	493	0.77	0.85	67	GSH, FAD, CL
2	77	0.42	0.80	16	empty
3	57	0.28	0.74	16	GOL

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

4NTD · Crystal structure of HlmI · 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 E2PZ87
Elsewhere: RCSB PDB 4NTD · PDBe 4NTD · UniProt E2PZ87

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