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Crystal Structure of MCR-1 Catalytic Domain

Analyse Crystal Structure of MCR-1 Catalytic Domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YLC
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.5
Source: Escherichia coli
Molecule: Probable phosphatidylethanolamine transferase Mcr-1
EC: 2.7.-.-
UniProt: A0A0R6L508
Ligands: ZN
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · resolution 1.5 · 1 distinct chain · 32% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable phosphatidylethanolamine transferase Mcr-1 (EC 2.7.-.-)	protein	330	32% helix, 17% strand	A0A0R6L508

Ligands and binding sites

ZN · Zinc ion · metal · 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	58	0.51	0.87	22	empty
2	97	0.42	0.78	18	empty

Modifications

Observed in the structure: 2 disulfide, 1 modified (disulfide, phosphorylation).

Compared structures

5YLC · Crystal structure of mcr-1 catalytic domain · 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 A0A0R6L508
Elsewhere: RCSB PDB 5YLC · PDBe 5YLC · UniProt A0A0R6L508

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