9GCP: ChREBP/14-3-3 complex stabilized by AMP

Name: PDB 9GCP: ChREBP/14-3-3 complex stabilized by AMP
Published: 2025-08-13
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

ChREBP/14-3-3 complex stabilized by AMP. Determined by X-ray diffraction at 2.59 Å resolution. Released 13 Aug 2025.

Method: X-ray diffraction
Resolution: 2.59 Å
Organism: Homo sapiens
Chains: 8
Atoms: 7,894
Mol. weight: 117.75 kDa
Ligands: AMP
Released: 13 Aug 2025

Explore 9GCP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GCP contains 57 α-helices and 0 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-32	12
α-helix	37-38	2
α-helix	40-68	29
α-helix	76-102	27
α-helix	103-107	5
α-helix	114-134	21
α-helix	138-161	24
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	205-207	3
α-helix	213-229	17

Chains B, F and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	118-135	18

Chain C: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-33	13
α-helix	37-38	2
α-helix	40-70	31
α-helix	76-102	27
α-helix	103-107	5
α-helix	114-134	21
α-helix	138-161	24
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	205-207	3
α-helix	213-230	18

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	118-134	17

Chain E: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-17	14
α-helix	21-33	13
α-helix	37-38	2
α-helix	40-69	30
α-helix	75-102	28
α-helix	103-107	5
α-helix	114-134	21
α-helix	137-161	25
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-202	16
α-helix	205-207	3
α-helix	213-231	19

Chain G: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	21-33	13
α-helix	37-38	2
α-helix	40-70	31
α-helix	76-102	27
α-helix	103-107	5
α-helix	108-110	3
α-helix	114-132	19
α-helix	138-161	24
α-helix	167-178	12
α-helix	179-183	5
α-helix	187-203	17
α-helix	205-207	3
α-helix	213-229	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein beta/alpha, N-terminally processed	A, C, E, G	protein	230	Homo sapiens	P31946 (AlphaFold model)
Carbohydrate-responsive element-binding protein	B, D, F, H	protein	20	Homo sapiens	Q9NP71 (AlphaFold model)

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

>9GCP_1 14-3-3 protein beta/alpha, N-terminally processed (chains A, C, E, G)
MDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWR
VISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLK
MKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYE
ILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTS

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

>9GCP_2 Carbohydrate-responsive element-binding protein (chains B, D, F, H)
RDKIRLNNAIWRAWYIQYVQ

Ligands and cofactors

ID	Name	Formula	Copies
AMP	Adenosine monophosphate	C10 H14 N5 O7 P	4

Primary citation

Glucose-6-phosphate functions as a selective receptor agonist for the sugar tolerance transcription factor ChREBP. Moschref, M., Heimhalt, M., Pysik, T. et al. To be published.

Other PDB entries of the same protein (UniProt P31946 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8EQ8 1.5 Å, The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y130
5N10 1.6 Å, Cucurbit[8]uril and 14-3-3 based binary bivalent supramolecular-protein assembly platform
6HEP 1.86 Å, Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768
8EQH 1.9 Å, The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y213
6A5Q 2.0 Å, Structure of 14-3-3 beta in complex with TFEB 14-3-3 binding motif
6YGJ 2.07 Å, small-molecule stabilizer of 14-3-3 and the Carbohydrate Response Element Binding…
4DNK 2.2 Å, Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation…
6GN8 2.34 Å, Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta,…
2BQ0 2.5 Å, 14-3-3 Protein Beta (Human)
6GNK 2.55 Å, Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta,…
2C23 2.65 Å, 14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide
6BYK 3.0 Å, Structure of 14-3-3 beta/alpha bound to O-ClcNAc peptide

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