2FF4: Mycobacterium tuberculosis EmbR

Mycobacterium tuberculosis EmbR in complex with low affinity phosphopeptide. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Jan 2006.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Mycobacterium tuberculosis
Chains: 4
Atoms: 6,377
Mol. weight: 86.06 kDa
Released: 24 Jan 2006

Explore 2FF4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2FF4 contains 37 α-helices and 40 β-strands across 4 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: 18 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	11-14	4	1
β-strand	20-23	4	1
β-strand	26-27	2	1
α-helix	33-44	12
β-strand	49-51	3	2
α-helix	52-60	9
α-helix	68-83	16
α-helix	84-86	3
α-helix	90-93	4
β-strand	94-96	3	2
β-strand	100-103	4	2
α-helix	107-109	3
β-strand	110	1	1
α-helix	111-127	17
α-helix	131-142	12
α-helix	151-153	3
α-helix	159-183	25
α-helix	187-200	14
α-helix	205-216	12
α-helix	221-239	19
α-helix	245-255	11
α-helix	262-280	19
β-strand	281	1	3
β-strand	287	1	3
α-helix	288-290	3
β-strand	291-294	4	4
β-strand	300-302	3	4
β-strand	307-311	5	5
β-strand	318-319	2	5
β-strand	330-334	5	5
β-strand	339-343	5	5
β-strand	351-352	2	4
β-strand	355-356	2	4
β-strand	360-363	4	5
α-helix	364	1
β-strand	368-371	4	4
β-strand	374-379	6	4
α-helix	382-383	2

Chain B: 17 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	11-14	4	6
β-strand	20-23	4	6
β-strand	26-27	2	6
α-helix	33-44	12
β-strand	50-51	2	7
α-helix	52-60	9
α-helix	68-83	16
α-helix	84-86	3
α-helix	90-93	4
β-strand	94-97	4	7
β-strand	100-103	4	7
α-helix	107-109	3
β-strand	110	1	6
α-helix	111-127	17
α-helix	131-143	13
α-helix	151-153	3
α-helix	159-183	25
α-helix	187-200	14
α-helix	205-217	13
α-helix	221-239	19
α-helix	242-244	3
α-helix	245-255	11
α-helix	262-280	19
β-strand	281	1	8
β-strand	287	1	8
α-helix	288-290	3
β-strand	291-294	4	9
β-strand	300-302	3	9
β-strand	307-311	5	10
β-strand	318-319	2	10
β-strand	330-334	5	10
β-strand	339-343	5	10
β-strand	351-352	2	9
β-strand	355-356	2	9
β-strand	361-362	2	10
β-strand	368-371	4	9
β-strand	374-379	6	9

Chains E and F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	4-7	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Probable regulatory protein embR	A, B	protein	388	Mycobacterium tuberculosis	P9WGJ9 (AlphaFold model)
DNA repair protein RAD9	E, F	protein	9		P14737 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2FF4_1 Probable regulatory protein embR (chains A, B)
MAGSATVEKRLDFGLLGPLQMTIDGTPVPSGTPKQRAVLAMLVINRNRPVGVDALITALW
EEWPPSGARASIHSYVSNLRKLLGGAGIDPRVVLAAAPPGYRLSIPDNTCDLGRFVAEKT
AGVHAAAAGRFEQASRHLSAALREWRGPVLDDLRDFQFVEPFATALVEDKVLAHTAKAEA
EIACGRASAVIAELEALTFEHPYREPLWTQLITAYYLSDRQSDALGAYRRVKTTLADDLG
IDPGPTLRALNERILRQQPLDAKKSAKTTAAGTVTVLDQRTMASGQQAVAYLHDIASGRG
YPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYVINDLRSSNGVHVQHERIRSA
VTLNDGDHIRICDHEFTFQISAGTHGGT

Sequence of entity 2 (E, F), FASTA

>2FF4_2 DNA repair protein RAD9 (chains E, F)
SLEVTEADT

Primary citation

Molecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis. Alderwick, L.J., Molle, V., Kremer, L. et al. Proc Natl Acad Sci U S A (2006) 103:2558-2563. DOI 10.1073/pnas.0507766103 · PubMed

Other PDB entries of the same protein (UniProt P9WGJ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2FEZ 2.0 Å, Mycobacterium tuberculosis EmbR

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