MolNFT v1 · #121140 · protein

Crystal structure of triazine hydrolase variant (P214T/Y215H/E241Q)

5HMF: “Crystal structure of triazine hydrolase variant (P214T/Y215H/E241Q)”. X-ray diffraction, 1 ligand (ZN), 7 pockets (best druggability 0.79). MolNFT v1 #121140 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5HMF
Type: protein
Length: 911 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triazine hydrolase
EC: 3.8.1.8
UniProt: Q6SJY7
Ligands: ZN
Pockets: 7 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Triazine hydrolase (EC 3.8.1.8)	protein	456	39% helix, 22% strand	Q6SJY7
B	Triazine hydrolase (EC 3.8.1.8)	protein	455	38% helix, 23% strand	Q6SJY7

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

7 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	121	0.79	0.98	35	empty
2	130	0.79	0.96	31	empty
3	322	0.75	0.86	53	empty
4	409	0.66	0.79	40	empty
5	92	0.43	0.78	19	empty

Interfaces

1 interface between chains.

A–B · 2729 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

5HMF · Crystal structure of triazine hydrolase variant (P214T/Y215H/E241Q) · 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 Q6SJY7
Elsewhere: RCSB PDB 5HMF · PDBe 5HMF · UniProt Q6SJY7

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