9SRW: Mlc tetramer

Cryo-EM structure of the Mlc tetramer in complex with the anti-repressor MtfA. Determined by electron microscopy at 2.3 Å resolution. Released 22 Jul 2026.

Method
Electron microscopy
Resolution
2.3 Å
Organism
Escherichia coli
Chains
6
Atoms
15,350
Mol. weight
266.06 kDa
Ligands
ZN
Released
22 Jul 2026

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

Secondary structure: helices and β-sheets

9SRW contains 108 α-helices and 80 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 and C: 21 helices, 20 β-strands

ElementResiduesLengthSheet
α-helix10-2819
β-strand3112
α-helix33-408
α-helix46-5611
β-strand60-6342
β-strand77-8042
β-strand86-9273
β-strand96-10383
β-strand108-11583
α-helix124-13815
α-helix139-1413
β-strand146-15383
β-strand156-15834
β-strand163-16644
β-strand17614
α-helix178-1869
β-strand190-19453
α-helix195-20511
β-strand215-21955
β-strand225-23065
β-strand233-23425
α-helix245-2473
β-strand24916
α-helix2551
β-strand25617
α-helix2571
β-strand26217
β-strand26416
α-helix266-2694
α-helix271-28313
α-helix289-2913
α-helix297-30610
α-helix309-33325
β-strand337-34155
α-helix343-3475
α-helix348-36114
α-helix365-3684
β-strand372-37545
α-helix383-3864
α-helix387-3959
α-helix400-4034
Chains B and D: 17 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix10-2819
α-helix33-397
α-helix44-5613
β-strand60-6238
β-strand78-8038
β-strand85-9289
β-strand96-10389
β-strand108-11589
α-helix124-13916
α-helix140-1423
β-strand145-15399
β-strand156-158310
β-strand163-166410
β-strand176110
α-helix178-1869
β-strand190-19459
α-helix195-20511
β-strand215-220611
β-strand224-230711
β-strand233-234211
α-helix245-2473
β-strand256112
β-strand262112
α-helix266-2694
α-helix271-28212
α-helix297-30610
α-helix309-33325
β-strand337-341511
α-helix343-3475
α-helix348-36114
α-helix365-3684
β-strand373-375311
α-helix385-39612
α-helix398-4047
Chains E and F: 16 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix19-224
α-helix26-283
α-helix33-4917
β-strand51-5331
α-helix63-7311
α-helix76-794
α-helix81-844
β-strand89-9351
α-helix1261
β-strand127-13041
α-helix131-1377
α-helix145-15410
α-helix173-19422
α-helix196-1983
α-helix203-2064
α-helix209-22214
α-helix224-2263
α-helix232-24211
α-helix246-2505

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Mlc titration factor AE, Fprotein287Escherichia coliP76346 (AlphaFold model)
DNA-binding transcriptional repressor MlcA, B, C, Dprotein455Escherichia coliP50456 (AlphaFold model)
Sequence of entity 1 (E, F), FASTA
>9SRW_1 Mlc titration factor A (chains E, F)
MIKWPWKVQESAHQTALPWQEALSIPLLTCLTEQEQSKLVTLAERFLQQKRLVPLQGFEL
DSLRSCRIALLFCLPVLELGLEWLDGFHEVLIYPAPFVVDDEWEDDIGLVHNQRIVQSGQ
SWQQGPIVLNWLDIQDSFDASGFNLIIHEVAHKLDTRNGDRASGVPFIPLREVAGWEHDL
HAAMNNIQEEIELVGENAASIDAYAASDPAECFAVLSEYFFSAPELFAPRFPSLWQRFCQ
FYQQDPLQRLHHANDTDSFSATNVHLELEVLFQGPVDHHHHHHHHHH
Sequence of entity 2 (A, B, C, D), FASTA
>9SRW_2 DNA-binding transcriptional repressor Mlc (chains A, B, C, D)
MGGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSELEVLFQGPKLMVAENQPGHIDQI
KQTNAGAVYRLIDQLGPVSRIDLSRLAQLAPASITKIVREMLEAHLVQELEIKEAGNRGR
PAVGLVVETEAWHYLSLRISRGEIFLALRDLSSKLVVEESQELALKDDLPLLDRIISHID
QFFIRHQKKLERLTSIAITLPGIIDTENGIVHRMPFYEDVKEMPLGEALEQHTGVPVYIQ
HDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGHTQVDPY
GKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSMLHGQPLTVDSLCQAALRGDLLAKD
IITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISV
ESTQFSNQGTMAGAALVKDAMYNGSLLIRLLQGLE

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn6

Primary citation

Structural basis of Mlc-mediated transcriptional regulation of carbohydrate metabolism. Roth, P., Fender, I., Jeckelmann, J.M. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-75270-8 · PubMed

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