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Crystal structure of escherichia COLI bamb, a lipoprotein component of the beta-barrel assembly machinery complex, native crystals.

Analyse Crystal structure of escherichia COLI bamb, a lipoprotein component of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P1L
Type: protein
Length: 361 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipoprotein yfgl
UniProt: P77774
Ligands: NA
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipoprotein yfgl	protein	361	0% helix, 47% strand	P77774

Ligands and binding sites

NA · Sodium ion · metal · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	388	0.61	0.77	35	NA
2	137	0.61	0.85	28	empty

Compared structures

3P1L · Crystal structure of Escherichia coli BamB, a lipoprotein component of the beta-barrel… · the same entry in another collection · chain A against A, TM-score 1.00
P77774 · AlphaFold monomer V2.0 prediction for outer membrane protein assembly factor bamb (P77774) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P77774
Elsewhere: RCSB PDB 3P1L · PDBe 3P1L · UniProt P77774

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