8BAV: Secretagogin

Secretagogin (human) in complex with its target peptide from SNAP-25. Determined by X-ray diffraction at 2.3 Å resolution. Released 3 Apr 2024.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Aequorea victoria, Homo sapiens
Chains: 4
Atoms: 8,620
Mol. weight: 122.69 kDa
Ligands: 144, CA
Released: 3 Apr 2024

Explore 8BAV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8BAV contains 47 α-helices and 40 β-strands across 4 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: 8 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	4-8	5
β-strand	12-22	11	1
β-strand	25-36	12	1
α-helix	37-39	3
β-strand	41-48	8	1
α-helix	57-60	4
α-helix	69-71	3
β-strand	73	1	1
α-helix	76-81	6
α-helix	83-86	4
β-strand	92-100	9	1
β-strand	105-115	11	1
β-strand	118-128	11	1
β-strand	141	1	2
β-strand	149-155	7	1
β-strand	160-170	11	1
β-strand	171	1	2
β-strand	176-187	12	1
α-helix	194-197	4
β-strand	199-208	10	1
β-strand	217-227	11	1
α-helix	233-244	12

Chain B: 8 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	4-8	5
β-strand	11-22	12	3
β-strand	25-36	12	3
α-helix	37-39	3
β-strand	41-48	8	3
α-helix	57-60	4
α-helix	69-71	3
β-strand	73	1	3
α-helix	76-81	6
α-helix	83-86	4
β-strand	92-100	9	3
β-strand	105-115	11	3
β-strand	118-128	11	3
β-strand	141	1	4
β-strand	148-155	8	3
β-strand	160-170	11	3
β-strand	171	1	4
β-strand	176-187	12	3
α-helix	194-197	4
β-strand	199-208	10	3
β-strand	217-227	11	3
α-helix	233-244	12

Chain C: 16 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	14-24	11
β-strand	31-33	3	5
α-helix	34-36	3
α-helix	37-47	11
α-helix	52-54	3
α-helix	55-68	14
β-strand	77-79	3	5
α-helix	80-87	8
α-helix	90-97	8
α-helix	107-117	11
β-strand	125	1	6
α-helix	127-140	14
α-helix	147-161	15
β-strand	169	1	6
α-helix	171-177	7
α-helix	184-187	4
α-helix	195-209	15
β-strand	216-217	2	7
α-helix	220-231	12
α-helix	239-253	15
β-strand	261-262	2	7
α-helix	263-269	7

Chain D: 15 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	14-24	11
β-strand	31	1	8
α-helix	37-47	11
α-helix	55-67	13
β-strand	79	1	8
α-helix	80-87	8
α-helix	90-97	8
α-helix	107-117	11
β-strand	125-126	2	9
α-helix	127-140	14
α-helix	147-161	15
β-strand	168-169	2	9
α-helix	171-177	7
α-helix	180-182	3
α-helix	184-187	4
α-helix	195-209	15
β-strand	216-217	2	10
α-helix	220-230	11
α-helix	239-253	15
β-strand	261-262	2	10
α-helix	263-269	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Green fluorescent protein,Synaptosomal-associated protein 25	A, B	protein	256	Aequorea victoria, Homo sapiens	P42212 (AlphaFold model), P60880 (AlphaFold model)
Secretagogin	C, D	protein	276	Homo sapiens	O76038 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8BAV_1 Green fluorescent protein,Synaptosomal-associated protein 25 (chains A, B)
SMASKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWP
TLVTTLXVQCFSRYPDHMKRHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLV
NRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKTRHNIEDGSVQLAD
HYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGTMAGIIGNLRHM
ALDMGNEIDTQNRQID

Sequence of entity 2 (C, D), FASTA

>8BAV_2 Secretagogin (chains C, D)
MDSSREPTLGRLDAAGFWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDDTVMKANLH
KVKQQFMTTQDASKDGRIRMKELAGMFLSEDENFLLLFRRENPLDSSVEFMQIWRKYDAD
SSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLARILAL
QENFLLQFKMDACSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGV
DLDKFREILLRHCDVNKDGKIQKSELALCLGLKINP

Ligands and cofactors

ID	Name	Formula	Copies
144	Tris-hydroxymethyl-methyl-ammonium	C4 H12 N O3	1
CA	Calcium ion	Ca	8

Water and common crystallization additives (ACT) are not listed.

Primary citation

A hydrophobic groove in secretagogin allows for alternate interactions with SNAP-25 and syntaxin-4 in endocrine tissues. Szodorai, E., Hevesi, Z., Wagner, L. et al. Proc Natl Acad Sci U S A (2024) 121:e2309211121-e2309211121. DOI 10.1073/pnas.2309211121 · PubMed

Other PDB entries of the same protein (UniProt P42212 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6L27 0.77 Å, X-ray crystal structure of the mutant green fluorescent protein
6JGJ 0.78 Å, Crystal structure of the F99S/M153T/V163A/E222Q variant of GFP at 0.78 A
6KL0 0.8 Å, Crystal structure of the S65T/F99S/M153T/V163A variant of perdeuterated GFP at pD 7.0
6JGI 0.85 Å, Crystal structure of the S65T/F99S/M153T/V163A variant of GFP at 0.85 A
6KL1 0.85 Å, Crystal structure of the S65T/F99S/M153T/V163A variant of non-deuterated GFP at pD 8.5
2WUR 0.9 Å, Atomic resolution structure of GFP measured on a rotating anode
6KKZ 0.9 Å, Crystal structure of the S65T/F99S/M153T/V163A variant of perdeuterated GFP at pD 8.5
6JGH 0.94 Å, Crystal structure of the F99S/M153T/V163A/T203I variant of GFP at 0.94 A
4AS8 1.02 Å, X-ray structure of the cyan fluorescent protein Cerulean cryoprotected with ethylene…
5OXC 1.02 Å, Structure of Cerulean Fluorescent Protein at 1.02 Angstrom resolution
7PCA 1.05 Å, Functional and structural characterization of redox sensitive superfolder green…
4GF6 1.1 Å, crystal structure of GFP with cuprum bound at the Incorporated metal Chelating Amino…

Browse structure collections

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