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Crystal structure of FAB15

Analyse Crystal structure of FAB15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NA9
Type: protein
Length: 439 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAB15 light chain; FAB15 heavy chain
Ligands: ZN
Pockets: 5 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	FAB15 light chain	protein	214	7% helix, 50% strand	—
H	FAB15 heavy chain	protein	225	9% helix, 52% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 7 copies · chains L, H
ACT · Acetate ion · additive · 4 copies · chains L, H
GOL · Glycerol · additive · 2 copies · chains L, H

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

Pockets

5 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	316	0.53	0.74	39	empty
2	87	0.44	0.79	18	empty
3	99	0.39	0.76	17	ZN, ACT
4	59	0.38	0.80	15	empty
5	69	0.28	0.73	19	empty

Interfaces

1 interface between chains.

L–H · 2059 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

3NA9 · Crystal structure of Fab15 · 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 3NA9 · PDBe 3NA9

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