1L1F: Human glutamate dehydrogenase-apo form

Structure of human glutamate dehydrogenase-apo form. Determined by X-ray diffraction at 2.7 Å resolution. Released 6 Mar 2002.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 6
Atoms: 23,244
Mol. weight: 336.51 kDa
Released: 6 Mar 2002

Explore 1L1F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1L1F contains 138 α-helices and 120 β-strands across 6 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.

Chains A, B, C, D, E and F: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	13-37	25
α-helix	38-40	3
α-helix	42-44	3
α-helix	46-49	4
α-helix	51-56	6
β-strand	61-70	10	1
β-strand	76-85	10	1
β-strand	93-96	4	2
β-strand	97-99	3	1
α-helix	105-121	17
β-strand	127-128	2	2
β-strand	129-133	5	1
α-helix	137-139	3
α-helix	142-158	17
β-strand	167-170	4	2
β-strand	172	1	3
β-strand	175	1	3
α-helix	177-189	13
α-helix	198-200	3
α-helix	207-209	3
α-helix	218-231	14
α-helix	234-240	7
β-strand	250-254	5	4
α-helix	258-269	12
β-strand	273-277	5	4
β-strand	278	1	5
β-strand	283	1	5
β-strand	285	1	6
α-helix	292-301	10
β-strand	312	1	6
β-strand	325-328	4	4
β-strand	335	1	7
α-helix	340-342	3
β-strand	347-349	3	4
β-strand	356	1	7
α-helix	358-366	9
β-strand	370-372	3	4
α-helix	374-377	4
α-helix	380-394	15
α-helix	403-422	20
α-helix	438-445	8
α-helix	449-474	26
α-helix	481-498	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamate Dehydrogenase 1	A, B, C, D, E, F	protein	505	Homo sapiens	P00367 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>1L1F_1 Glutamate Dehydrogenase 1 (chains A, B, C, D, E, F)
SEAVADREDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCN
HVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCA
VVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREM
SWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSIL
GMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKL
QHGSILGFPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEA
DKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQES
LERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLD
LRTAAYVNAIEKVFKVYNEAGVTFT

Primary citation

The structure of apo human glutamate dehydrogenase details subunit communication and allostery. Smith, T.J., Schmidt, T., Fang, J. et al. J Mol Biol (2002) 318:765-777. DOI 10.1016/S0022-2836(02)00161-4 · PubMed

Other PDB entries of the same protein (UniProt P00367 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8SK8 2.31 Å, human liver mitochondrial Glutamate dehydrogenase 1
8KGY 2.59 Å, Human glutamate dehydrogenase I
6DQG 2.7 Å, Human glutamate dehydrogenase, H454Y mutant
8W4J 3.06 Å, Cryo-EM structure of the KLHL22 E3 ligase bound to human glutamate dehydrogenase I
7UZM 3.24 Å, Glutamate dehydrogenase 1 from human liver
1NR1 3.3 Å, Crystal structure of the R463A mutant of human Glutamate dehydrogenase

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