MolNFT v1 · #99223 · protein

Conserved residues that modulate protein trans-splicing of npu dnae split intein

4LX3 · DNA polymerase III, alpha subunit: “Conserved residues that modulate protein trans-splicing of npu dnae split intein”. X-ray diffraction, 1 pocket (best druggability 0.41). MolNFT v1 #99223 on GenesisL1: 3D structure, binding sites…

PDB: 4LX3
Type: protein
Length: 137 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA polymerase III, alpha subunit; Nucleic acid binding, ob-fold, TRNA/HELICASE-type
EC: 2.7.7.7
UniProt: B2J066, B2J821
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA polymerase III, alpha subunit (EC 2.7.7.7)	protein	101	12% helix, 47% strand	B2J066
B	Nucleic acid binding, ob-fold, TRNA/HELICASE-type (EC 2.7.7.7)	protein	36	8% helix, 64% strand	B2J821

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	75	0.41	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 2432 Å² buried · 51 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

4LX3 · Conserved Residues that Modulate Protein trans-Splicing of Npu DnaE Split Intein · 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 B2J066
Every structure of UniProt B2J821
Elsewhere: RCSB PDB 4LX3 · PDBe 4LX3 · UniProt B2J066 · UniProt B2J821

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