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Muconate lactonizing enzyme from pseudomonas putida

Analyse Muconate lactonizing enzyme from pseudomonas putida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BKH
Type: protein
Length: 1,078 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Muconate lactonizing enzyme
EC: 5.5.1.1
Pockets: 8 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Muconate lactonizing enzyme (EC 5.5.1.1)	protein	358	43% helix, 20% strand	—
B	Muconate lactonizing enzyme (EC 5.5.1.1)	protein	361	43% helix, 22% strand	—
C	Muconate lactonizing enzyme (EC 5.5.1.1)	protein	359	43% helix, 21% strand	—

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	835	0.83	0.86	82	empty
2	383	0.60	0.77	57	empty
3	186	0.50	0.77	38	empty
4	113	0.50	0.80	22	empty
5	116	0.48	0.79	18	empty

Interfaces

2 interfaces between chains.

A–C · 1037 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 295 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1BKH · Muconate lactonizing enzyme from pseudomonas putida · 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
Elsewhere: RCSB PDB 1BKH · PDBe 1BKH

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