MolNFT v1 · #141812 · protein

Crystal structure of the catalytic domain of mcr-1 (cmcr-1) in complex with xylose

5ZJV · Probable phosphatidylethanolamine transferase mcr-1: “Crystal structure of the catalytic domain of mcr-1 (cmcr-1) in complex with xylose”. X-ray diffraction, 2 ligands (LXC, ZN), 2 pockets (best druggability 0.55). MolNFT v1 #141812…

PDB: 5ZJV
Type: protein
Length: 331 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable phosphatidylethanolamine transferase mcr-1
EC: 2.7.-.-
UniProt: A0A0R6L508
Ligands: LXC, ZN
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable phosphatidylethanolamine transferase mcr-1 (EC 2.7.-.-)	protein	331	31% helix, 17% strand	A0A0R6L508

Ligands and binding sites

LXC · beta-L-xylopyranose · sugar · chains A
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	61	0.55	0.88	22	empty
2	68	0.32	0.76	14	empty

Modifications

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

Compared structures

5ZJV · Crystal structure of the catalytic domain of MCR-1 (cMCR-1) in complex with xylose · 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 5ZJV · PDBe 5ZJV · UniProt A0A0R6L508

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