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Structure of bame from neisseria gonorrhoeae

Analyse Structure of bame from neisseria gonorrhoeae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WAM
Type: protein
Length: 200 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer membrane protein assembly factor bame
UniProt: Q5F5Y8
Ligands: ZN
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Outer membrane protein assembly factor bame	protein	103	28% helix, 38% strand	Q5F5Y8
B	Outer membrane protein assembly factor bame	protein	97	26% helix, 39% strand	Q5F5Y8

Ligands and binding sites

ZN · Zinc ion · metal · chains A, B

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

Pockets

2 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	234	0.59	0.80	42	empty
2	56	0.27	0.72	13	empty

Interfaces

1 interface between chains.

A–B · 1289 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

5WAM · Structure of BamE from Neisseria gonorrhoeae · 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 Q5F5Y8
Elsewhere: RCSB PDB 5WAM · PDBe 5WAM · UniProt Q5F5Y8

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