MolNFT v1 · #101613 · protein

Crystal structure of APE1551, an anti-human ngf Fab with a nine amino acid insertion in cdr H1

4NWU · APE1551 ab Fab heavy chain: “Crystal structure of APE1551, an anti-human ngf Fab with a nine amino acid insertion in cdr H1”. X-ray diffraction, 3 pockets (best druggability 0.63). MolNFT v1 #101613 on GenesisL1: 3D structure…

PDB: 4NWU
Type: protein
Length: 451 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: APE1551 ab Fab heavy chain; APE1551 ab Fab light chain
UniProt: P01857, Q8TCD0
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	APE1551 ab Fab heavy chain	protein	231	9% helix, 53% strand	P01857
L	APE1551 ab Fab light chain	protein	220	5% helix, 52% strand	Q8TCD0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	589	0.63	0.75	58	empty
2	201	0.52	0.77	30	empty
3	62	0.30	0.74	15	empty

Interfaces

1 interface between chains.

H–L · 2126 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

4NWU · Crystal structure of APE1551, an anti-human NGF Fab with a nine amino acid insertion in… · the same entry in another collection · chain H against H, 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 P01857
Every structure of UniProt Q8TCD0
Elsewhere: RCSB PDB 4NWU · PDBe 4NWU · UniProt P01857 · UniProt Q8TCD0

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