9GIW: Mitochondrial pyruvate carrier 1-like protein

Structure of the human mitochondrial pyruvate carrier inhibited by zaprinast. Determined by electron microscopy at 3.92 Å resolution. Released 7 May 2025.

Method: Electron microscopy
Resolution: 3.92 Å
Organisms: Homo sapiens, synthetic construct
Chains: 3
Atoms: 2,661
Mol. weight: 86.83 kDa
Ligands: A1IL3
Released: 7 May 2025

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

Secondary structure: helices and β-sheets

9GIW contains 14 α-helices and 11 β-strands across 3 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: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	18-25	8
α-helix	27-47	21
α-helix	50-52	3
α-helix	55-74	20
α-helix	80-104	25

Chain B: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	9-23	15
α-helix	29-32	4
α-helix	41-60	20
α-helix	69-88	20
α-helix	94-120	27

Chain C: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	1
β-strand	13-14	2	2
β-strand	21-28	8	1
α-helix	30-35	6
α-helix	37-39	3
β-strand	41-47	7	2
β-strand	54-59	6	2
β-strand	66-68	3	2
β-strand	76-81	6	1
β-strand	86-91	6	1
α-helix	96-98	3
β-strand	100-107	8	2
α-helix	115-117	3
β-strand	120-121	2	2
β-strand	125-128	4	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitochondrial pyruvate carrier 1-like protein	A	protein	136	Homo sapiens	P0DKB6 (AlphaFold model)
Mitochondrial pyruvate carrier 2	B	protein	133	Homo sapiens	O95563 (AlphaFold model)
Nanobody,Maltose/maltodextrin-binding periplasmic protein	C	protein	515	synthetic construct	P0AEY0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9GIW_1 Mitochondrial pyruvate carrier 1-like protein (chains A)
MARMAVLWRKMRDNFQSKEFREYVSSTHFWGPAFSWGLPLAAFKDMKASPEIISGRMTTA
LILYSAIFMRFAYRVQPRNLLLMACHCTNVMAQSVQASRYLLYYYGGGGAEAKARDPPAT
AAAATSPGSQPPKQAS

Sequence of entity 2 (B), FASTA

>9GIW_2 Mitochondrial pyruvate carrier 2 (chains B)
MSAAGARGLRATYHRLLDKVELMLPEKLRPLYNHPAGPRTVFFWAPIMKWGLVCAGLADM
ARPAEKLSTAQSAVLMATGFIWSRYSLVIIPKNWSLFAVNFFVGAAGASQLFRIWRYNQE
LKAKAHKENLYFQ

Sequence of entity 3 (C), FASTA

>9GIW_3 Nanobody,Maltose/maltodextrin-binding periplasmic protein (chains C)
GPSQVQLVESGGGLVQAGGSLRLSCAASGRTFSAYGISTYTMGWFRQAPGKEREFVAAIG
RDSGFTYYEDSVKGRFTINADNAENTVYLQMNSLKPEDTAVYYCAASSYYGRPNVDLMAY
WGKGTQVTVPPLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGD
GPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSL
IYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGK
YDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI
DTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNK
DKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQ
TVDEALKDAQTPGSPDAAIEGRTSEDAWSHPQFEK

Ligands and cofactors

ID	Name	Formula	Copies
A1IL3	5-(2-propoxyphenyl)-3,4-dihydro-[1,2,3]triazolo[4,5-d]pyrimidin-7-one	C13 H13 N5 O2	1

Primary citation

Molecular basis of pyruvate transport and inhibition of the human mitochondrial pyruvate carrier. Sichrovsky, M., Lacabanne, D., Ruprecht, J.J. et al. Sci Adv (2025) 11:eadw1489-eadw1489. DOI 10.1126/sciadv.adw1489 · PubMed

Other PDB entries of the same protein (UniProt P0DKB6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9GIV 3.65 Å, Structure of the human mitochondrial pyruvate carrier inhibited by a UK5099-derivative
9GIX 3.65 Å, Structure of the human mitochondrial pyruvate carrier in the apo-state
9GIY 3.79 Å, Structure of the human mitochondrial pyruvate carrier inhibited by mitoglitazone

Browse structure collections

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