3J07: Model of a 24mer alphaB-crystallin multimer

Model of a 24mer alphaB-crystallin multimer. Determined by solid-state NMR at 20.0 Å resolution. Released 20 Jan 2016.

Method: Solid-state NMR
Resolution: 20.0 Å
Organism: Homo sapiens
Chains: 24
Atoms: 33,912
Mol. weight: 484.61 kDa
Released: 20 Jan 2016

Explore 3J07 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3J07 contains 81 α-helices and 168 β-strands across 24 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: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
α-helix	15-17	3
α-helix	24-34	11
β-strand	49	1	1
β-strand	62	1	1
β-strand	76-77	2	2
β-strand	89-94	6	3
β-strand	97-108	12	3
β-strand	112-122	11	3
β-strand	136-137	2	4
β-strand	143-144	2	4
β-strand	145-146	2	2

Chain B: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	15-17	3
α-helix	26-36	11
β-strand	76-78	3	5
β-strand	89-94	6	3
β-strand	97-108	12	3
β-strand	112-122	11	3
β-strand	136-137	2	5
β-strand	143-146	4	5

Chains C and G: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	6-9	4
α-helix	15-17	3
α-helix	24-34	11
β-strand	49	1	6
β-strand	62	1	6
β-strand	78-79	2	7
β-strand	89-94	6	8
β-strand	97-108	12	8
β-strand	112-122	11	8
β-strand	136-137	2	7
β-strand	143-144	2	7

Chain D: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	15-17	3
α-helix	27-31	5
α-helix	33-36	4
β-strand	76-78	3	9
β-strand	89-94	6	8
β-strand	97-108	12	8
β-strand	112-122	11	8
β-strand	136-137	2	9
β-strand	143-146	4	9

Chain E: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
α-helix	15-17	3
α-helix	24-34	11
β-strand	49	1	10
β-strand	62	1	10
α-helix	65-67	3
β-strand	76-78	3	11
β-strand	89-94	6	12
β-strand	97-108	12	12
β-strand	112-122	11	12
β-strand	136-137	2	11
β-strand	143-146	4	11

Chains F, T and X: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	15-17	3
α-helix	27-36	10
β-strand	76-78	3	13
β-strand	89-94	6	12
β-strand	97-108	12	12
β-strand	112-122	11	12
β-strand	136	1	13
β-strand	144-146	3	13

Chain H: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
α-helix	15-17	3
α-helix	27-31	5
α-helix	33-36	4
β-strand	76-78	3	17
β-strand	89-94	6	16
β-strand	97-108	12	16
β-strand	112-122	11	16
β-strand	137	1	18
β-strand	143	1	18
β-strand	144-146	3	17

Chain I: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
α-helix	15-17	3
α-helix	24-34	11
β-strand	49	1	19
β-strand	62	1	19
β-strand	78-79	2	20
β-strand	89-94	6	21
β-strand	97-108	12	21
β-strand	112-122	11	21
β-strand	136-137	2	20
β-strand	143-144	2	20

12 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-crystallin B chain	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X	protein	175	Homo sapiens	P02511 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X), FASTA

>3J07_1 Alpha-crystallin B chain (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X)
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSW
FDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHR
KYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK

Primary citation

N-terminal domain of {alpha}B-crystallin provides a conformational switch for multimerization and structural heterogeneity. Jehle, S., Vollmar, B.S., Bardiaux, B. et al. Proc Natl Acad Sci U S A (2011) 108:6409-6414. DOI 10.1073/pnas.1014656108 · PubMed

Other PDB entries of the same protein (UniProt P02511 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4M5S 1.37 Å, Human alphaB crystallin core domain in complex with C-terminal peptide
3SGP 1.4 Å, Amyloid-related segment of alphaB-crystallin residues 90-100 mutant V91L
7ROJ 1.6 Å, Amyloid-related segment of alphaB-crystallin residues 90-100 with G95W mutation
3SGM 1.7 Å, Bromoderivative-2 of amyloid-related segment of alphaB-crystallin residues 90-100
3SGS 1.7 Å, Amyloid-related segment of alphaB-crystallin residues 95-100
2Y1Y 2.0 Å, Human alphaB crystallin ACD(residues 71-157)
4M5T 2.0 Å, Disulfide trapped human alphaB crystallin core domain in complex with C-terminal peptide
3SGR 2.17 Å, Tandem repeat of amyloid-related segment of alphaB-crystallin residues 90-100 mutant V91L
2Y1Z 2.5 Å, Human alphaB Crystallin ACD R120G
3SGO 2.56 Å, Amyloid-related segment of alphaB-crystallin residues 90-100
2WJ7 2.63 Å, human alphaB crystallin
5VVV 2.8 Å, Structural Investigations of the Substrate Specificity of Human O-GlcNAcase

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