3BX7: Engineered Human Lipocalin 2

Engineered Human Lipocalin 2 (LCN2) in Complex with the Extracellular Domain of Human CTLA-4. Determined by X-ray diffraction at 2.1 Å resolution. Released 20 Jan 2009.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,473
Mol. weight: 33.5 kDa
Released: 20 Jan 2009

Explore 3BX7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BX7 contains 14 α-helices and 22 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: 10 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	7-12	6
α-helix	13-15	3
α-helix	24-27	4
β-strand	29-38	10	3
α-helix	48-49	2
β-strand	50	1	4
α-helix	51	1
β-strand	53-58	6	3
β-strand	64-72	9	3
β-strand	75-85	11	3
β-strand	91-94	4	3
α-helix	97-99	3
β-strand	105-113	9	3
β-strand	118-127	10	3
β-strand	130-139	10	3
α-helix	146-158	13
α-helix	163-165	3
β-strand	166-167	2	3
α-helix	169	1
β-strand	170	1	4
α-helix	171	1

Chain C: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	1
β-strand	10-12	3	2
β-strand	19-24	6	1
β-strand	33-42	10	2
β-strand	45-54	10	2
β-strand	59	1	1
α-helix	62-63	2
β-strand	68-73	6	1
β-strand	76-81	6	1
α-helix	86-88	3
β-strand	90-100	11	2
α-helix	104	1
β-strand	105-108	4	2
β-strand	112-115	4	2
α-helix	118-120	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytotoxic T-lymphocyte-associated antigen 4	C	protein	124	Homo sapiens	P16410 (AlphaFold model)
Engineered human lipocalin 2	A	protein	178	Homo sapiens

Sequence of entity 1 (C), FASTA

>3BX7_1 CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 4 (chains C)
MHVAQPAVVLASSRGIASFVCEYASPGKATEVRVTVLRQADSQVTEVCAATYMMGNELTF
LDDSICTGTSSGNQVNLTIQGLRAMDTGLYICKVELMYPPPYYLGIGNGTQIYVIDPEPC
PDSD

Sequence of entity 2 (A), FASTA

>3BX7_2 ENGINEERED HUMAN LIPOCALIN 2 (chains A)
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGKWYVVGLAGNRILRDDQHPMNMYATIYELKE
DKSYNVTSVISSHKKCEYTIATFVPGSQPGEFTLGNIKSYGDKTSYLVRVVSTDYNQYAV
VFFKLAEDNAEFFAITIYGRTKELASELKENFIRFSKSLGLPENHIVFPVPIDQCIDG

Primary citation

High affinity molecular recognition and functional blockade of CTLA-4 by an engineered human lipocalin. Schonfeld, D.L., Matschiner, G., Chatwell, L. et al. To be published.

Other PDB entries of the same protein (UniProt P16410 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7CIO 1.1 Å, Molecular interactions of cytoplasmic region of CTLA-4 with SH2 domains of PI3-kinase
9DQ3 1.64 Å, Crystal structure of engineered Ipilimumab (mipi.4) Fab in complex with human CTLA-4
3OSK 1.8 Å, Crystal structure of human CTLA-4 apo homodimer
5GGV 2.0 Å, CTLA-4 in complex with tremelimumab Fab
7ELX 2.14 Å, The crystal structure of CTLA-4 and Fab
7DV4 2.38 Å, Crystal structure of anti-CTLA-4 VH domain in complex with human CTLA-4
7SU0 2.41 Å, Crystal structure of an acidic pH-selective Ipilimumab variant Ipi.105 in complex with…
7SU1 2.53 Å, Crystal structure of an acidic pH-selective Ipilimumab variant Ipi.106 in complex with…
2X44 2.6 Å, Structure of a strand-swapped dimeric form of CTLA-4
6RP8 2.6 Å, Crystal Structure of Ipilimumab Fab complexed with CTLA-4 at 2.6A resolution
8GAB 2.72 Å, Crystal structure of CTLA-4 in complex with a high affinity CTLA-4 binder
1I8L 3.0 Å, Human B7-1/CTLA-4 co-stimulatory complex

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