3BZE: PDB entry 3BZE

The human non-classical major histocompatibility complex molecule HLA-E. Determined by X-ray diffraction at 2.5 Å resolution. Released 29 Apr 2008.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 12
Atoms: 12,744
Mol. weight: 178.27 kDa
Released: 29 Apr 2008

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

Secondary structure: helices and β-sheets

3BZE contains 52 α-helices and 116 β-strands across 8 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, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	1
β-strand	21-28	8	1
β-strand	31-37	7	1
β-strand	46-47	2	1
α-helix	50-52	3
α-helix	57-84	28
β-strand	94-103	10	1
β-strand	109-118	10	1
β-strand	121-126	6	1
β-strand	133-135	3	1
α-helix	138-140	3
α-helix	141-149	9
α-helix	153-158	6
α-helix	159-163	5
α-helix	164-174	11
α-helix	176-179	4
β-strand	183	1	2
α-helix	184-185	2
β-strand	186-193	8	3
β-strand	198-208	11	3
β-strand	209	1	2
β-strand	214-218	5	4
β-strand	229-230	2	3
β-strand	234-235	2	3
β-strand	241-250	10	3
α-helix	254-256	3
β-strand	258-262	5	4
β-strand	270-272	3	4

Chains B and F: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	5
α-helix	4-5	2
β-strand	6-11	6	6
β-strand	21-30	10	6
β-strand	31	1	5
β-strand	36-41	6	7
β-strand	44-45	2	7
β-strand	50-51	2	6
α-helix	52-54	3
β-strand	55-56	2	6
β-strand	62-70	9	6
β-strand	78-83	6	7
β-strand	91-94	4	7

Chain C: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-14	12	8
β-strand	18-28	11	8
β-strand	31-37	7	8
β-strand	46-47	2	8
α-helix	50-52	3
α-helix	59-84	26
β-strand	94-103	10	8
β-strand	109-118	10	8
β-strand	121-126	6	8
β-strand	133-135	3	8
α-helix	141-149	9
α-helix	153-158	6
α-helix	159-164	6
α-helix	165-174	10
α-helix	176-179	4
β-strand	183	1	9
α-helix	184-185	2
β-strand	186-193	8	10
β-strand	198-208	11	10
β-strand	209	1	9
β-strand	214-219	6	11
β-strand	228-230	3	10
α-helix	231-233	3
β-strand	234-235	2	10
β-strand	241-250	10	10
α-helix	254-256	3
β-strand	257-262	6	11
β-strand	270-272	3	11

Chain D: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	12
α-helix	4-5	2
β-strand	6-11	6	13
β-strand	21-30	10	13
β-strand	31	1	12
β-strand	36-41	6	14
β-strand	44-45	2	14
α-helix	46	1
β-strand	50-51	2	13
β-strand	55-56	2	13
β-strand	62-70	9	13
β-strand	78-83	6	14
β-strand	91-94	4	14

Chain E: 12 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	15
α-helix	20	1
β-strand	21-28	8	15
β-strand	31-37	7	15
β-strand	46-47	2	15
α-helix	50-52	3
α-helix	57-84	28
β-strand	94-103	10	15
β-strand	109-118	10	15
β-strand	121-126	6	15
β-strand	133-135	3	15
α-helix	141-150	10
α-helix	152-154	3
α-helix	155-157	3
α-helix	158-163	6
α-helix	164-174	11
α-helix	176-179	4
β-strand	183	1	16
α-helix	184-185	2
β-strand	186-195	10	17
β-strand	198-208	11	17
β-strand	209	1	16
β-strand	214-219	6	18
β-strand	230	1	17
α-helix	231-233	3
β-strand	234-235	2	17
β-strand	241-249	9	17
α-helix	254-256	3
β-strand	257-262	6	18
β-strand	270-272	3	18

Chain G: 13 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	22
α-helix	15-17	3
β-strand	21-28	8	22
β-strand	31-37	7	22
β-strand	46-47	2	22
α-helix	50-52	3
α-helix	57-84	28
β-strand	94-103	10	22
β-strand	109-118	10	22
β-strand	121-126	6	22
β-strand	133-135	3	22
α-helix	138-140	3
α-helix	141-149	9
α-helix	153-158	6
α-helix	159-163	5
α-helix	164-174	11
α-helix	176-179	4
β-strand	183	1	23
α-helix	184-185	2
β-strand	186-193	8	24
β-strand	198-208	11	24
β-strand	209	1	23
β-strand	214-219	6	25
α-helix	227-228	2
β-strand	229-230	2	24
α-helix	231-233	3
β-strand	234-235	2	24
β-strand	241-250	10	24
α-helix	254-256	3
β-strand	257-262	6	25
β-strand	270-272	3	25

Chain H: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	26
α-helix	4-5	2
β-strand	6-11	6	27
β-strand	21-30	10	27
β-strand	31	1	26
β-strand	36-41	6	28
β-strand	44-45	2	28
β-strand	50-51	2	27
β-strand	55-56	2	27
β-strand	62-70	9	27
β-strand	78-83	6	28
β-strand	91-94	4	28

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HLA class I histocompatibility antigen, alpha chain E	A, C, E, G	protein	273	Homo sapiens	P13747 (AlphaFold model)
Beta-2-microglobulin	B, D, F, H	protein	100	Homo sapiens	P61769 (AlphaFold model)
leader peptide of HLA class I histocompatibility antigen, alpha chain G	P, Q, R, S	protein	9		P17693 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>3BZE_1 HLA class I histocompatibility antigen, alpha chain E (chains A, C, E, G)
SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWD
RETRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDRRFLRGYEQFAYDGK
DYLTLNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLH
LEPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTF
QKWAAVVVPSGEEQRYTCHVQHEGLPEPVTLRW

Sequence of entity 2 (B, D, F, H), FASTA

>3BZE_2 Beta-2-microglobulin (chains B, D, F, H)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (P, Q, R, S), FASTA

>3BZE_3 leader peptide of HLA class I histocompatibility antigen, alpha chain G (chains P, Q, R, S)
VMAPRTLFL

Primary citation

Subtle changes in peptide conformation profoundly affect recognition of the non-classical MHC class I molecule HLA-E by the CD94-NKG2 natural killer cell receptors. Hoare, H.L., Sullivan, L.C., Clements, C.S. et al. J Mol Biol (2008) 377:1297-1303. DOI 10.1016/j.jmb.2008.01.098 · PubMed

Other PDB entries of the same protein (UniProt P13747 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7P4B 1.72 Å, HLA-E*01:03 in complex with IL9
7BH8 1.8 Å, 3H4-Fab HLA-E-VL9 co-complex
7P49 2.05 Å, HLA-E*01:03 in complex with Mtb14
6GH1 2.1 Å, HLA-E*01:03 in complex with Mtb44
9NW7 2.1 Å, CA117v2v8 Fab bound to HLA-E-VL9
6GH4 2.16 Å, HLA-E*01:03 in complex with the Mtb44 peptide variant: Mtb44*P2-Gln.
6ZKX 2.17 Å, Crystal structure of InhA:01 TCR in complex with HLA-E (Y84C) bound to InhA (53-61 GCG)
8RLT 2.25 Å, TCR in complex with HLA-E*01:03 bound to HBV envelope 371-379 index peptide
6ZKW 2.26 Å, Crystal structure of InhA:01 TCR in complex with HLA-E bound to InhA (53-61)
6ZKZ 2.3 Å, Crystal structure of InhA:01 TCR in complex with HLA-E (F116C) bound to InhA (53-61 H4C)
9NW8 2.3 Å, CA117v2v8 Fab bound to HLA-E-Mtb44
9NW9 2.3 Å, CA117v2v8 Fab bound to HLA-E-RL9HIV

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