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High-resolution structure of txte with bound tryptophan substrate

Analyse High-resolution structure of txte with bound tryptophan substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TPO
Type: protein
Length: 398 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative P450-like protein
UniProt: C9ZDC6
Ligands: HEM, TRP, SO4
Pockets: 3 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative P450-like protein	protein	398	53% helix, 10% strand	C9ZDC6

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
TRP · Tryptophan · ligand · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
GOL · Glycerol · additive · 3 copies · 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	801	0.86	0.89	79	HEM, TRP
2	172	0.44	0.74	22	SO4
3	83	0.35	0.75	15	empty

Compared structures

4TPO · High-resolution structure of TxtE with bound tryptophan substrate · 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 C9ZDC6
Elsewhere: RCSB PDB 4TPO · PDBe 4TPO · UniProt C9ZDC6

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