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Structure of PA1221, an nrps protein containing adenylation and pcp domains

Analyse Structure of PA1221, an nrps protein containing adenylation and pcp domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DG8
Type: protein
Length: 495 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PA1221
EC: 6.2.1.-
UniProt: Q9I4B7
Ligands: AMP
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PA1221 (EC 6.2.1.-)	protein	495	31% helix, 29% strand	Q9I4B7

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
BU3 · (R,R)-2,3-butanediol · additive · 2 copies · chains A

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

Pockets

5 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	829	0.80	0.82	86	AMP, BU3
2	113	0.43	0.77	20	empty
3	72	0.37	0.78	19	empty
4	60	0.31	0.76	16	empty
5	54	0.28	0.75	13	empty

Compared structures

4DG8 · Structure of PA1221, an NRPS protein containing adenylation and PCP domains · 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 Q9I4B7
Elsewhere: RCSB PDB 4DG8 · PDBe 4DG8 · UniProt Q9I4B7

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