MolNFT v1 · #146070 · protein

Structure of polyribonucleotide nucleotidyltransferase from acinetobacter baumannii

6D6K: “Structure of polyribonucleotide nucleotidyltransferase from acinetobacter baumannii”. X-ray diffraction, 8 pockets (best druggability 0.77). MolNFT v1 #146070 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6D6K
Type: protein
Length: 1,095 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polyribonucleotide nucleotidyltransferase
EC: 2.7.7.8
UniProt: V5VH92
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polyribonucleotide nucleotidyltransferase (EC 2.7.7.8)	protein	543	32% helix, 31% strand	V5VH92
B	Polyribonucleotide nucleotidyltransferase (EC 2.7.7.8)	protein	552	34% helix, 28% strand	V5VH92

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	945	0.77	0.80	84	empty
2	860	0.75	0.79	88	empty
3	529	0.60	0.74	63	empty
4	416	0.57	0.74	49	empty
5	149	0.48	0.77	28	empty

Interfaces

1 interface between chains.

A–B · 649 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6D6K · Structure of polyribonucleotide nucleotidyltransferase from Acinetobacter baumannii · 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 V5VH92
Elsewhere: RCSB PDB 6D6K · PDBe 6D6K · UniProt V5VH92

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