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PAPA2 acyl transferase

Analyse PAPA2 acyl transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AEF
Type: protein
Length: 916 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polyketide synthase associated protein PAPA2
UniProt: R4MC47
Ligands: ZN
Pockets: 7 · best druggability 0.90

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Polyketide synthase associated protein PAPA2	protein	458	41% helix, 25% strand	R4MC47

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains B, A
ACT · Acetate ion · additive · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

7 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	902	0.90	0.92	136	empty
2	215	0.59	0.81	28	empty
3	90	0.52	0.84	17	empty
4	56	0.47	0.85	15	empty
5	166	0.47	0.76	29	empty

Interfaces

1 interface between chains.

B–A · 968 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

6AEF · PapA2 acyl transferase · the same entry in another collection · chain B against B, 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 R4MC47
Elsewhere: RCSB PDB 6AEF · PDBe 6AEF · UniProt R4MC47

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