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Hydrolase semet-stna

Analyse Hydrolase semet-stna in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HDF
Type: protein
Length: 1,267 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrolase
UniProt: L7PIJ2
Pockets: 12 · best druggability 0.71

Structure

x-ray diffraction · 3 distinct chains · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Hydrolase	protein	320	36% helix, 21% strand	L7PIJ2
A	Hydrolase	protein	315	36% helix, 22% strand	L7PIJ2
C, D	Hydrolase	protein	316	36% helix, 22% strand	L7PIJ2

Pockets

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1117	0.71	0.76	74	empty
2	268	0.69	0.84	30	empty
3	241	0.68	0.85	32	empty
4	245	0.66	0.83	30	empty
5	251	0.66	0.83	31	empty

Interfaces

3 interfaces between chains.

B–C · 498 Å² buried · 3 hydrogen bonds · protein-protein
B–A · 443 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 147 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 28 modified, 8 disulfide (engineered, disulfide).

Compared structures

5HDF · Hydrolase SeMet-StnA · the same entry in another collection · chain D against D, 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 L7PIJ2
Elsewhere: RCSB PDB 5HDF · PDBe 5HDF · UniProt L7PIJ2

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