4NUJ: HIV-1 broadly neutralizing antibody PGT152

Crystal structure of HIV-1 broadly neutralizing antibody PGT152. Determined by X-ray diffraction at 1.83 Å resolution. Released 14 May 2014.

Method: X-ray diffraction
Resolution: 1.83 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,955
Mol. weight: 50.08 kDa
Released: 14 May 2014

Explore 4NUJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4NUJ contains 16 α-helices and 46 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-13	4	2
β-strand	19-25	7	1
β-strand	27C	1	3
β-strand	31	1	3
β-strand	33-38	6	2
β-strand	45-49	5	2
β-strand	53-54	2	2
α-helix	55	1
β-strand	62-67	6	1
β-strand	70-75	6	1
α-helix	80-82	3
β-strand	84-90	7	2
α-helix	96	1
β-strand	97-98	2	2
β-strand	102-106	5	2
β-strand	111	1	4
α-helix	112-113	2
β-strand	114-118	5	5
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	5
β-strand	140	1	4
β-strand	145-150	6	6
β-strand	153-154	2	6
α-helix	155	1
β-strand	159-163	5	5
α-helix	164-167	4
β-strand	173-182	10	5
α-helix	183-188	6
β-strand	191-197	7	6
β-strand	205-210	6	6

Chain B: 7 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	7
β-strand	11-12	2	8
β-strand	18-25	8	7
α-helix	29-31	3
β-strand	34-39	6	9
β-strand	45-51	7	9
β-strand	57-59	3	9
β-strand	67-72	6	7
β-strand	77-82	6	7
α-helix	84-86	3
β-strand	88-95	8	9
β-strand	100R-103	4	9
β-strand	107-109	3	9
β-strand	110-111	2	8
β-strand	117	1	10
α-helix	118-119	2
β-strand	120-124	5	11
β-strand	135-145	11	11
β-strand	146	1	10
β-strand	151-154	4	12
α-helix	155-157	3
β-strand	159	1	12
β-strand	163-165	3	11
α-helix	166-168	3
β-strand	169-170	2	11
β-strand	176-185	10	11
α-helix	186-188	3
β-strand	195-200	6	12
α-helix	201-203	3
β-strand	205-210	6	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PGT152 light chain	A	protein	219	Homo sapiens	Q8TCD0 (AlphaFold model)
PGT152 heavy chain	B	protein	240	Homo sapiens	Q6N089 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4NUJ_1 PGT152 light chain (chains A)
DIVMTQTPLSLSVDPGQPASISCKSSQSLRQSNGKTSLYWYQQKPGQSPQLLIFEVSNRF
SGVSDRFVGSGSGTDFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLKRTVAAPSV
FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 2 (B), FASTA

>4NUJ_2 PGT152 heavy chain (chains B)
RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISADAWHVVY
SGSVQGRFLVSRDNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNYYYYS
GMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGA
LTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDK

Primary citation

Structural Delineation of a Quaternary, Cleavage-Dependent Epitope at the gp41-gp120 Interface on Intact HIV-1 Env Trimers. Blattner, C., Lee, J.H., Sliepen, K. et al. Immunity (2014) 40:669-680. DOI 10.1016/j.immuni.2014.04.008 · PubMed

Other PDB entries of the same protein (UniProt Q8TCD0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4NWU 1.6 Å, Crystal structure of APE1551, an anti-human NGF Fab with a nine amino acid insertion in…
6ARP 1.7 Å, Structure of a mutant Cetuximab Fab fragment
6DC4 1.7 Å, RSV-neutralizing human antibody AM22
4NWT 1.75 Å, Crystal structure of the anti-human NGF Fab APE1531
6UC5 1.75 Å, Fab397 in complex with NPNA peptide
3MNZ 1.8 Å, Crystal structure of the non-neutralizing HIV antibody 13H11 Fab fragment with a gp41…
4NUG 1.86 Å, Crystal structure of HIV-1 broadly neutralizing antibody PGT151
5VKK 2.01 Å, Crystal structure of Fab fragment of anti-CD22 Epratuzumab
3PGF 2.1 Å, Crystal structure of maltose bound MBP with a conformationally specific synthetic…
3MNW 2.2 Å, Crystal structure of the non-neutralizing HIV antibody 13H11 Fab fragment with a gp41…
6E4X 2.25 Å, Human antibody S5V2-29 in complex with influenza hemagglutinin A/Texas/50/2012 (H3N2)
4D9Q 2.28 Å, Inhibiting Alternative Pathway Complement Activation by Targeting the Exosite on Factor D

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