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Native crystal structure of the recombinant monoclonal wild type anti-testosterone Fab fragment

Analyse Native crystal structure of the recombinant monoclonal wild type… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1I9I
Type
protein
Length
439 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Recombinant monoclonal anti-testosterone Fab fragment light chain; Recombinant monoclonal…
UniProt
Q99M37, Q9R1A4
Pockets
3 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LRecombinant monoclonal anti-testosterone Fab fragment light chainprotein2195% helix, 51% strandQ99M37
HRecombinant monoclonal anti-testosterone Fab fragment heavy chainprotein2205% helix, 49% strandQ9R1A4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15710.630.7560empty
23750.610.7746empty
3750.300.7319empty

Interfaces

1 interface between chains.

  • L–H · 1953 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 1I9I · Native crystal structure of the recombinant monoclonal wild type anti-testosterone Fab… · the same entry in another collection · chain L against L, TM-score 1.00

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