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Crystal structure of pseudomonas sp. P51 chloromuconate lactonizing enzyme

Analyse Crystal structure of pseudomonas sp. P51 chloromuconate lactonizing enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NU5
Type: protein
Length: 369 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chloromuconate cycloisomerase
EC: 5.5.1.7
UniProt: P27099
Ligands: MN
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chloromuconate cycloisomerase (EC 5.5.1.7)	protein	369	42% helix, 24% strand	P27099

Ligands and binding sites

MN · Manganese (II) ion · metal · 2 copies · chains A

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

Pockets

2 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	411	0.66	0.79	55	empty
2	74	0.46	0.82	19	empty

Compared structures

1NU5 · Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme · the same entry in another collection · chain A against A, TM-score 1.00
P27099 · AlphaFold monomer V2.0 prediction for chloromuconate cycloisomerase (P27099) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P27099
Elsewhere: RCSB PDB 1NU5 · PDBe 1NU5 · UniProt P27099

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