MolNFT v1 · #9659 · protein

Crystal structure of an ampicillin single chain fv, form 1, free

1I3G · Antibody fv fragment: “Crystal structure of an ampicillin single chain fv, form 1, free”. X-ray diffraction, 4 pockets (best druggability 0.58). MolNFT v1 #9659 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1I3G
Type: protein
Length: 217 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antibody fv fragment
Pockets: 4 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	Antibody fv fragment	protein	106	3% helix, 47% strand	—
H	Antibody fv fragment	protein	111	5% helix, 53% strand	—

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains L, H

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

Pockets

4 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	179	0.58	0.81	21	MPD
2	96	0.36	0.74	23	empty
3	69	0.29	0.73	16	empty
4	58	0.27	0.73	19	empty

Interfaces

1 interface between chains.

L–H · 697 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1I3G · Crystal structure of an ampicillin single chain fv, form 1, free · the same entry in another collection · chain L against L, 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
Elsewhere: RCSB PDB 1I3G · PDBe 1I3G

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