MolNFT v2 · #157679 · protein

Cleaved Ebola GP in complex with a broadly neutralizing human antibody, ADI-15946

6MAM: “Cleaved Ebola GP in complex with a broadly neutralizing human antibody, ADI-15946”. X-ray diffraction at 4.1, 3 ligands (NAG, MAN, BMA). MolNFT v2 #157679 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6MAM
Type: protein
Length: 2,131 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 4.1
Source: Homo sapiens; Zaire ebolavirus (strain Mayinga-76)
UniProt: Q05320
Ligands: NAG, MAN, BMA

Structure

x-ray diffraction · resolution 4.1 · 10 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	226	—	—
B, D	—	protein	215	—	—
C	—	protein	233	—	—
E	—	protein	235	—	—
F	—	protein	216	—	—
G	—	protein	157	—	Q05320
H	—	protein	108	—	Q05320
I, K	—	protein	156	—	Q05320
J	—	protein	109	—	Q05320
L	—	protein	105	—	Q05320

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains G, H, J, I, K, L
MAN · alpha-D-mannopyranose · sugar · 5 copies
BMA · beta-D-mannopyranose · sugar · 3 copies

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

Compared structures

6MAM · Cleaved ebola gp in complex with a broadly neutralizing human antibody, adi-15946 · 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 Q05320
Elsewhere: RCSB PDB 6MAM · PDBe 6MAM · UniProt Q05320

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