5ZAB: Cf3-aequorin

Crystal structure of cf3-aequorin. Determined by X-ray diffraction at 2.15 Å resolution. Released 6 Jun 2018.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Aequorea victoria
Chains: 16
Atoms: 26,420
Mol. weight: 368.83 kDa
Ligands: 9A3
Released: 6 Jun 2018

Explore 5ZAB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5ZAB contains 188 α-helices and 66 β-strands across 16 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: 11 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
β-strand	30-32	3	1
α-helix	33-46	14
α-helix	52-68	17
β-strand	76-78	3	1
α-helix	79-98	20
α-helix	101-103	3
α-helix	104-116	13
β-strand	123-124	2	2
α-helix	126-136	11
α-helix	142-151	10
β-strand	160-161	2	2
α-helix	162-170	9
α-helix	171-175	5
α-helix	178-180	3

Chains B and I: 11 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
β-strand	30-32	3	3
α-helix	33-46	14
α-helix	52-68	17
β-strand	76-78	3	3
α-helix	79-98	20
α-helix	101-103	3
α-helix	104-116	13
β-strand	123-124	2	4
α-helix	126-136	11
α-helix	142-151	10
β-strand	160-161	2	4
α-helix	162-169	8
α-helix	170-175	6
α-helix	178-180	3

Chain C: 12 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
β-strand	30-32	3	5
α-helix	33-42	10
α-helix	43-47	5
α-helix	52-67	16
β-strand	76-78	3	5
α-helix	79-98	20
α-helix	101-103	3
α-helix	104-116	13
β-strand	123-124	2	6
α-helix	126-136	11
α-helix	142-151	10
β-strand	160-161	2	6
α-helix	162-169	8
α-helix	170-175	6
α-helix	178-180	3

Chains D and H: 12 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
β-strand	30-32	3	7
α-helix	33-41	9
α-helix	42-47	6
α-helix	52-68	17
β-strand	76-78	3	7
α-helix	79-98	20
α-helix	101-103	3
α-helix	104-116	13
β-strand	123-124	2	8
α-helix	126-136	11
α-helix	142-151	10
β-strand	160-161	2	8
α-helix	162-170	9
α-helix	171-175	5
α-helix	178-180	3

Chain E: 12 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
β-strand	30-32	3	9
α-helix	33-41	9
α-helix	42-47	6
α-helix	52-68	17
β-strand	76-78	3	9
α-helix	79-98	20
α-helix	101-103	3
α-helix	104-116	13
β-strand	123-124	2	10
α-helix	126-136	11
α-helix	142-151	10
β-strand	160-161	2	10
α-helix	162-169	8
α-helix	170-175	6
α-helix	178-180	3

Chain F: 12 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	-1	1	11
α-helix	10-23	14
β-strand	30-32	3	12
α-helix	33-42	10
α-helix	43-47	5
α-helix	52-68	17
β-strand	76-78	3	12
α-helix	79-98	20
α-helix	101-103	3
α-helix	104-116	13
β-strand	123-124	2	13
α-helix	126-136	11
α-helix	142-151	10
β-strand	160-161	2	13
α-helix	162-170	9
α-helix	171-175	5
α-helix	178-180	3

Chain G: 11 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	11
α-helix	10-23	14
β-strand	30-32	3	14
α-helix	33-48	16
α-helix	52-67	16
β-strand	76-78	3	14
α-helix	79-98	20
α-helix	101-103	3
α-helix	104-116	13
β-strand	123-124	2	15
α-helix	126-136	11
α-helix	142-152	11
β-strand	160-161	2	15
α-helix	162-170	9
α-helix	171-175	5
α-helix	178-180	3

Chain J: 12 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
β-strand	30-32	3	20
α-helix	33-41	9
α-helix	42-47	6
α-helix	52-68	17
β-strand	76-78	3	20
α-helix	79-98	20
α-helix	101-103	3
α-helix	104-116	13
β-strand	123-124	2	21
α-helix	126-136	11
α-helix	142-152	11
β-strand	160-161	2	21
α-helix	162-169	8
α-helix	170-175	6
α-helix	178-180	3

5 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
Aequorin-2	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	protein	198	Aequorea victoria	P02592 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P), FASTA

>5ZAB_1 Aequorin-2 (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P)
ANSHHHHHHGKLTSDFDNPRWIGRHKHMFNFLDVNHNGKISLDEMVYKASDIVINNLGAT
PEQAKRHKDAVEAFFGGAGMKYGVETDWPAYIEGWKKLATDELEKYAKNEPTLIRIWGDA
LFDIVDKDQNGAITLDEWKAYTKAAGIIQSSEDCEETFRVCDIDESGQLDVDEMTRQHLG
FWYTMDPACEKLYGGAVP

Ligands and cofactors

ID	Name	Formula	Copies
9A3	(2S)-8-benzyl-2-hydroperoxy-6-(4-hydroxyphenyl)-2-{[4-(trifluoromethyl)phenyl]m…	C27 H20 F3 N3 O4	16

Primary citation

Slow luminescence kinetics of semi-synthetic aequorin: expression, purification and structure determination of cf3-aequorin. Inouye, S., Tomabechi, Y., Hosoya, T. et al. J Biochem (2018) 164:247-255. DOI 10.1093/jb/mvy049 · PubMed

Other PDB entries of the same protein (UniProt P02592 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1UHK 1.6 Å, Crystal structure of n-aequorin
1UHH 1.8 Å, Crystal structure of cp-aequorin
1UHI 1.8 Å, Crystal structure of i-aequorin
1UHJ 1.8 Å, Crystal structure of br-aequorin
7EG3 2.09 Å, Crystal structure of the apoAequorin complex with (S)-HM-daCTZ
7EG2 2.22 Å, Crystal structure of the apoAequorin complex with (S)-daCTZ
1EJ3 2.3 Å, Crystal structure of aequorin

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