1I10: L-lactate dehydrogenase M chain

Human muscle L-lactate dehydrogenase M chain, ternary complex with NADH and oxamate. Determined by X-ray diffraction at 2.3 Å resolution. Released 28 Mar 2001.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
8
Atoms
21,581
Mol. weight
299.34 kDa
Ligands
NAI, OXM
Released
28 Mar 2001

Explore 1I10 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I10 contains 131 α-helices and 123 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: 17 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix3-75
β-strand8-1031
β-strand21-2552
α-helix29-4012
β-strand46-5052
α-helix54-6512
α-helix68-703
β-strand75-7842
α-helix82-854
β-strand90-9342
α-helix99-1002
α-helix105-1084
α-helix109-12618
β-strand131-13442
α-helix139-15012
α-helix154-1563
β-strand157-15932
α-helix163-17715
α-helix181-1833
β-strand18513
β-strand188-18924
β-strand19012
β-strand197-19824
α-helix200-2023
β-strand204-20523
β-strand208-20923
α-helix210-2134
α-helix227-24418
α-helix249-26315
β-strand268-27582
β-strand287-29592
β-strand298-30362
α-helix309-32618
Chain B: 17 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix3-75
β-strand8-1035
β-strand21-2556
α-helix29-4012
β-strand46-5056
α-helix54-6512
α-helix68-703
β-strand75-7846
α-helix82-854
β-strand88-9366
α-helix105-1084
α-helix109-12618
α-helix1301
β-strand131-13446
α-helix139-15012
α-helix154-1563
β-strand157-15936
α-helix163-17715
α-helix181-1833
β-strand18517
β-strand188-18928
β-strand19016
β-strand197-19828
α-helix200-2023
β-strand204-20527
β-strand208-20927
α-helix210-2134
α-helix227-24418
α-helix249-26315
β-strand268-27586
β-strand287-29596
β-strand298-30366
α-helix309-32719
Chain C: 17 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix3-75
β-strand8-1036
β-strand21-2555
α-helix29-4012
β-strand46-5055
α-helix54-6613
α-helix68-703
β-strand75-7845
α-helix82-854
β-strand90-9345
α-helix105-1084
α-helix109-12618
α-helix1301
β-strand131-13445
α-helix139-15012
α-helix154-1563
β-strand157-15935
α-helix163-17715
α-helix181-1833
β-strand18519
β-strand188-189210
β-strand19015
β-strand197-198210
α-helix200-2023
β-strand204-20529
β-strand208-20929
α-helix210-2134
α-helix227-24418
α-helix249-26315
β-strand268-27585
β-strand287-29595
β-strand298-30365
α-helix309-32719
Chain D: 17 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix3-75
β-strand8-1032
β-strand21-2551
α-helix29-4012
β-strand46-5051
α-helix54-6613
α-helix68-703
β-strand75-7841
α-helix82-854
β-strand90-9341
α-helix97-993
α-helix106-12621
α-helix1301
β-strand131-13441
α-helix139-15012
α-helix154-1563
β-strand157-15931
α-helix163-17715
α-helix181-1833
β-strand184-185211
β-strand188-19031
β-strand196-19831
α-helix200-2023
β-strand204-205211
β-strand208-209211
α-helix210-2134
α-helix227-24418
α-helix249-26315
β-strand268-27581
β-strand287-296101
β-strand298-30361
α-helix309-32618
Chain E: 16 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix3-75
β-strand8-10312
β-strand21-25513
α-helix29-3911
β-strand46-50513
α-helix54-6512
α-helix68-703
β-strand76-78313
α-helix82-854
β-strand90-93413
α-helix109-12618
α-helix1301
β-strand131-134413
α-helix139-15012
α-helix154-1563
β-strand157-159313
α-helix163-17614
α-helix181-1833
β-strand185114
β-strand188-190313
β-strand196-198313
α-helix200-2023
β-strand204-205214
β-strand208-209214
α-helix227-2348
α-helix236-2449
α-helix249-26315
β-strand268-275813
β-strand287-295913
β-strand298-303613
α-helix312-32817
Chain F: 16 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix3-75
β-strand8-10315
β-strand21-25516
α-helix29-3911
β-strand46-50516
α-helix54-6613
α-helix68-703
β-strand75-78416
α-helix82-854
β-strand90-93416
α-helix105-1084
α-helix109-12618
α-helix1301
β-strand131-134416
α-helix139-15012
α-helix154-1563
β-strand157-159316
α-helix163-17715
α-helix181-1833
β-strand185-189517
β-strand190116
β-strand197-205917
β-strand208-209217
α-helix210-2134
α-helix227-24418
α-helix249-26315
β-strand268-275816
β-strand287-295916
β-strand298-303616
α-helix309-32921
Chain G: 14 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix3-75
β-strand8-10316
β-strand21-25515
α-helix29-4012
β-strand46-50515
α-helix54-6512
α-helix68-703
β-strand75-78415
α-helix82-854
β-strand90-93415
α-helix108-12619
β-strand131-134415
α-helix139-15012
α-helix154-1563
β-strand157-159315
α-helix163-17715
α-helix181-1833
β-strand184-185218
β-strand188-190315
β-strand196-198315
α-helix200-2023
β-strand204-205218
β-strand208-209218
α-helix228-24417
α-helix249-26315
β-strand268-275815
β-strand287-295915
β-strand298-303615
α-helix309-32719
Chain H: 17 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix3-75
β-strand8-10313
β-strand21-25512
α-helix29-4012
β-strand46-50512
α-helix54-6613
α-helix68-703
β-strand75-78412
α-helix82-854
β-strand90-93412
α-helix99-1002
α-helix105-1084
α-helix109-12618
β-strand131-134412
α-helix139-15012
α-helix154-1563
β-strand157-159312
α-helix163-17715
α-helix181-1833
β-strand185119
β-strand188-189220
β-strand190112
β-strand197-198220
α-helix200-2023
β-strand204-205219
β-strand208-209219
α-helix210-2134
α-helix227-24418
α-helix249-26315
β-strand268-275812
β-strand287-295912
β-strand298-303612
α-helix309-32921

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
L-lactate dehydrogenase M chainA, B, C, D, E, F, G, Hprotein331Homo sapiensP00338 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>1I10_1 L-LACTATE DEHYDROGENASE M CHAIN (chains A, B, C, D, E, F, G, H)
ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGE
MMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII
PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVH
PLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV
IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGIS
DLVKVTLTSEEEARLKKSADTLWGIQKELQF

Ligands and cofactors

IDNameFormulaCopies
NAI1,4-dihydronicotinamide adenine dinucleotideC21 H29 N7 O14 P28
OXMOxamic acidC2 H3 N O38

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

Primary citation

Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Read, J.A., Winter, V.J., Eszes, C.M. et al. Proteins (2001) 43:175-185. DOI 10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-# · PubMed

Other PDB entries of the same protein (UniProt P00338 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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