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Crystal structure of mycolic acid cyclopropane synthase CMAA1, apo-form

Analyse Crystal structure of mycolic acid cyclopropane synthase CMAA1, apo-form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KP9
Type: protein
Length: 540 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclopropane-fatty-acyl-phospholipid synthase 1
EC: 2.1.1.79
UniProt: Q11195
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cyclopropane-fatty-acyl-phospholipid synthase 1 (EC 2.1.1.79)	protein	270	43% helix, 17% strand	Q11195

Ligands and binding sites

ACY · Acetic acid · additive · 3 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	840	0.79	0.82	79	empty
2	517	0.74	0.82	52	ACY
3	518	0.74	0.82	51	ACY

Interfaces

1 interface between chains.

A–B · 568 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1KP9 · Crystal structure of mycolic acid cyclopropane synthase CmaA1, apo-form · 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 Q11195
Elsewhere: RCSB PDB 1KP9 · PDBe 1KP9 · UniProt Q11195

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