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Crystal structure of beta-carboxy-CIS,CIS-muconate cycloisomerase (cmle) from acinetobacter calcoaceticus sp. ADP1

Analyse Crystal structure of beta-carboxy-CIS,CIS-muconate cycloisomerase (cmle) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q5N
Type: protein
Length: 431 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-carboxy-CIS,CIS-muconate cycloisomerase
EC: 5.5.1.2
UniProt: Q59092
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-carboxy-CIS,CIS-muconate cycloisomerase (EC 5.5.1.2)	protein	431	70% helix, 4% strand	Q59092

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	147	0.59	0.83	23	empty
2	100	0.38	0.75	24	empty

Compared structures

1Q5N · Crystal Structure of beta-carboxy-cis,cis-muconate cycloisomerase (CMLE) from… · the same entry in another collection · chain A against A, TM-score 1.00
Q59092 · AlphaFold monomer V2.0 prediction for 3-carboxy-CIS,CIS-muconate cycloisomerase (Q59092) · a predicted model of the same protein · 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 Q59092
Elsewhere: RCSB PDB 1Q5N · PDBe 1Q5N · UniProt Q59092

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