1NMU: Mbp-L30

Mbp-L30. Determined by X-ray diffraction at 2.31 Å resolution. Released 18 Feb 2003.

Method: X-ray diffraction
Resolution: 2.31 Å
Organisms: Escherichia coli, Saccharomyces cerevisiae
Chains: 4
Atoms: 7,593
Mol. weight: 107.61 kDa
Released: 18 Feb 2003

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

Secondary structure: helices and β-sheets

1NMU contains 55 α-helices and 56 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: 23 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	1
α-helix	17-31	15
β-strand	34-38	5	1
α-helix	43-51	9
β-strand	59-63	5	1
α-helix	64-66	3
α-helix	67-72	6
β-strand	76	1	2
α-helix	77-79	3
α-helix	83-86	4
β-strand	89	1	3
α-helix	91-96	6
β-strand	98-99	2	4
β-strand	102-103	2	4
β-strand	106-111	6	1
β-strand	114-118	5	5
β-strand	128	1	6
α-helix	132-140	9
β-strand	145-147	3	5
α-helix	154-163	10
β-strand	167-172	6	7
β-strand	175-182	8	7
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	5
α-helix	229-231	3
α-helix	232-237	6
β-strand	242-245	4	5
α-helix	246-248	3
β-strand	249	1	6
β-strand	250	1	8
β-strand	253	1	8
α-helix	257	1
β-strand	258-259	2	9
β-strand	260-266	7	1
β-strand	267	1	2
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	1
β-strand	304	1	3
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	9
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-368	12

Chain B: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
β-strand	22-25	4	10
α-helix	26-35	10
β-strand	41-45	5	10
α-helix	53-62	10
β-strand	67-70	4	10
α-helix	79-87	9
β-strand	89-94	6	10
α-helix	100-104	5

Chain C: 23 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	11
α-helix	17-31	15
β-strand	35-38	4	11
α-helix	43-51	9
β-strand	59-63	5	11
α-helix	64-66	3
α-helix	67-72	6
β-strand	76	1	12
α-helix	83-86	4
β-strand	89	1	13
α-helix	91-96	6
β-strand	98-99	2	14
β-strand	102-103	2	14
β-strand	106-111	6	11
β-strand	114-118	5	15
β-strand	128	1	16
α-helix	129-131	3
α-helix	132-140	9
β-strand	145-147	3	15
α-helix	154-163	10
β-strand	167-171	5	17
β-strand	176-182	7	17
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	15
α-helix	229-231	3
α-helix	232-236	5
β-strand	242-245	4	15
α-helix	246-248	3
β-strand	249	1	16
β-strand	250	1	18
β-strand	253	1	18
α-helix	257	1
β-strand	258-259	2	19
β-strand	260-266	7	11
β-strand	267	1	12
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-294	8
β-strand	301-302	2	11
β-strand	304	1	13
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	19
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-368	12

Chain D: 4 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	8-20	13
β-strand	22-25	4	20
α-helix	27-36	10
β-strand	41-44	4	20
α-helix	52-62	11
β-strand	66-69	4	20
α-helix	74-80	7
β-strand	89-94	6	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
maltose-binding periplasmic protein	A, C	protein	382	Escherichia coli	P0AEX9 (AlphaFold model)
60S ribosomal protein L30	B, D	protein	104	Saccharomyces cerevisiae	P14120 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1NMU_1 maltose-binding periplasmic protein (chains A, C)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE
ALKDAQTNSSSVPGRGSIEGRA

Sequence of entity 2 (B, D), FASTA

>1NMU_2 60S ribosomal protein L30 (chains B, D)
APVKSQESINQKLALVIKSGKYTLGYKSTVKSLRQGKSKLIIIAANTPVLRKSELEYYAM
LSKTKVYYFQGGNNELGTAVGKLFRVGVVSILEAGDSDILTTLA

Primary citation

Inherent Protein Structural Flexibility at the RNA-binding Interface of L30e. Chao, J.A., Prasad, G.S., White, S.A. et al. J Mol Biol (2003) 326:999-1004. DOI 10.1016/S0022-2836(02)01476-6 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8C8F 1.15 Å, Crystal structure of the E. coli maltodextrin-binding protein
4EXK 1.28 Å, A chimera protein containing MBP fused to the C-terminal domain of the uncharacterized…
3Q27 1.3 Å, Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
7KD4 1.31 Å, Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329…
5M13 1.37 Å, Synthetic nanobody in complex with MBP
5HZ7 1.43 Å, High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria…
5H7Q 1.45 Å, Crystal structure of human MNDA PYD domain with MBP tag
6XDS 1.47 Å, Crystal structure of MBP-TREM2 Ig domain fusion with fragment,…
4IRL 1.47 Å, X-ray structure of the CARD domain of zebrafish GBP-NLRP1 like protein
8SVY 1.47 Å, MBP-Mcl1 in complex with ligand 10
3MP6 1.48 Å, Complex Structure of Sgf29 and dimethylated H3K4
9CLC 1.48 Å, Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Cyanotryptophan

Browse structure collections

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