3BES: Poxvirus ifngbp/ifng Complex

Structure of a Poxvirus ifngbp/ifng Complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 12 Feb 2008.

Method: X-ray diffraction
Resolution: 2.2 Å
Organisms: Homo sapiens, Ectromelia virus
Chains: 2
Atoms: 3,420
Mol. weight: 46.15 kDa
Ligands: NAG, PO4
Released: 12 Feb 2008

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

Secondary structure: helices and β-sheets

3BES contains 20 α-helices and 19 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 L: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	2-14	13
α-helix	20-23	4
α-helix	30-35	6
α-helix	39-58	20
α-helix	67-80	14
α-helix	86-97	12
α-helix	103-120	18
α-helix	123-125	3

Chain R: 12 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	18-26	9	1
β-strand	29-36	8	1
β-strand	40-46	7	2
β-strand	53-59	7	2
β-strand	62-65	4	1
β-strand	77-83	7	2
β-strand	86-92	7	2
α-helix	95-98	4
β-strand	100	1	1
β-strand	105-111	7	3
β-strand	114-120	7	3
α-helix	121-122	2
β-strand	123-126	4	4
β-strand	129-132	4	4
α-helix	137-139	3
α-helix	144	1
β-strand	145-152	8	5
α-helix	158	1
β-strand	159-162	4	5
α-helix	163-164	2
α-helix	165-167	3
β-strand	168	1	3
β-strand	172-177	6	3
β-strand	183-190	8	5
β-strand	198	1	5
α-helix	199-204	6
β-strand	205-207	3	5
α-helix	209-211	3
α-helix	221-223	3
α-helix	224-238	15
α-helix	241-263	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interferon gamma	L	protein	139	Homo sapiens	P01579 (AlphaFold model)
Interferon-gamma binding protein C4R	R	protein	250	Ectromelia virus	Q66793 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>3BES_1 Interferon gamma (chains L)
MQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKN
FKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAE
LSPAAKTGKRKRSQMLFRG

Sequence of entity 2 (R), FASTA

>3BES_2 Interferon-gamma binding protein C4R (chains R)
TITSYKFESVNFDSKIEWTGNGLYNISLRNYGIKTWQTMYTNVPEGTYDISGFPNNDFVS
FWVKFEQGDYKVDKYCTGLCIEVKIGPPTVTLTEYDDHINLYIEHPYATRGSKKIPIYKR
NDMCDIYLLYTANFTFGDSEEPVIYDIDDYDCTSTGCSIDFATTEKVCVMAQGATEGLLD
KITPWSSEVCLTPKKNVYTCAIRSKEDVPNFKEKMTRVIKRKFNKQSHSYLTKFLGSTSN
DITTFLSMLD

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
PO4	Phosphate ion	O4 P	3

Primary citation

Structure and mechanism of IFN-gamma antagonism by an orthopoxvirus IFN-gamma-binding protein. Nuara, A.A., Walter, L.J., Logsdon, N.J. et al. Proc Natl Acad Sci U S A (2008) 105:1861-1866. DOI 10.1073/pnas.0705753105 · PubMed

Other PDB entries of the same protein (UniProt P01579 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1FYH 2.04 Å, 1:1 complex between an interferon gamma single-chain variant and its receptor
1EKU 2.9 Å, Crystal structure of a biologically active single chain mutant of human ifn-gamma
1FG9 2.9 Å, 3:1 complex of interferon-gamma receptor with interferon-gamma dimer
9VNP 3.02 Å, The complexes of IFN-gamma and A01BM-03 Fab
6E3K 3.25 Å, Interferon gamma signalling complex with IFNGR1 and IFNGR2
1HIG 3.5 Å, Three-dimensional structure of recombinant human interferon-gamma.
6E3L 3.8 Å, Interferon gamma signalling complex with IFNGR1 and IFNGR2

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