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Structure of rvfv gn and human monoclonal antibody R17

Analyse Structure of rvfv gn and human monoclonal antibody R17 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IEC
Type: protein
Length: 2,108 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nsmgngc; R17 H chain; R17 L chain
UniProt: H9BSP3
Pockets: 20 · best druggability 0.65

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, E, I	Nsmgngc	protein	301	13% helix, 29% strand	H9BSP3
H, C, F, J	R17 H chain	protein	115	3% helix, 43% strand	—
L, D, G, K	R17 L chain	protein	111	5% helix, 43% strand	—

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	492	0.65	0.77	47	empty
2	468	0.65	0.77	47	empty
3	268	0.58	0.78	35	empty
4	238	0.58	0.79	37	empty
5	140	0.57	0.83	23	empty

Interfaces

17 interfaces between chains.

F–G · 905 Å² buried · 10 hydrogen bonds · protein-protein
J–K · 903 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 903 Å² buried · 10 hydrogen bonds · protein-protein
H–L · 903 Å² buried · 10 hydrogen bonds · protein-protein
B–E · 585 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 44 disulfide (disulfide).

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Every structure of UniProt H9BSP3
Elsewhere: RCSB PDB 6IEC · PDBe 6IEC · UniProt H9BSP3

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