5B00: Prenyltransferase MoeN5

Name: PDB 5B00: Structure of the prenyltransferase MoeN5 in complex with geranyl pyrophosphate
Published: 2016-03-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Structure of the prenyltransferase MoeN5 in complex with geranyl pyrophosphate. Determined by X-ray diffraction at 2.95 Å resolution. Released 23 Mar 2016.

Method: X-ray diffraction
Resolution: 2.95 Å
Organism: Streptomyces ghanaensis
Chains: 3
Atoms: 6,233
Mol. weight: 97.72 kDa
Ligands: GPP
Released: 23 Mar 2016

Explore 5B00 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5B00 contains 48 α-helices and 0 β-strands across 3 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: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	0-17	18
α-helix	26-30	5
α-helix	33-42	10
α-helix	49-74	26
α-helix	81-101	21
α-helix	108-115	8
α-helix	117-129	13
α-helix	135-137	3
α-helix	143-148	6
α-helix	149-159	11
α-helix	167-189	23
α-helix	202-205	4
α-helix	211-230	20
α-helix	238-248	11
α-helix	249-253	5
α-helix	254-256	3

Chain B: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	0-17	18
α-helix	26-30	5
α-helix	33-42	10
α-helix	49-74	26
α-helix	81-101	21
α-helix	108-115	8
α-helix	117-129	13
α-helix	142	1
α-helix	143-148	6
α-helix	149-159	11
α-helix	167-188	22
α-helix	202-205	4
α-helix	211-230	20
α-helix	238-248	11
α-helix	249-253	5
α-helix	254-256	3

Chain C: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	0-17	18
α-helix	25-30	6
α-helix	33-42	10
α-helix	49-74	26
α-helix	81-101	21
α-helix	108-115	8
α-helix	117-129	13
α-helix	135-138	4
α-helix	143-148	6
α-helix	149-159	11
α-helix	167-188	22
α-helix	202-205	4
α-helix	211-230	20
α-helix	238-248	11
α-helix	249-253	5
α-helix	254-256	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MoeN5	A, B, C	protein	294	Streptomyces ghanaensis	A0A010 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>5B00_1 MoeN5 (chains A, B, C)
MAHHHHHHVDDDDKAASWSHPQFEKGAENLYFQSMLAAEAANRDHVTRCVAQTGGSPDLV
AHTAALRLYLRVPHFLTEWTTDPDRRAAVSRALALDIVSMKLLDDLMDDDTGLDRVELAC
VCLRLHLRALHELESLARDPKAVTDILEQDAVHLCGGQIRTKRSRATNLREWRAHASTYG
STFLGRYGALAAACGGEGQPADSVREFAEAFAMTITMADDLTDYDRNGERDGNLAHLMRT
GAVAGQDVVDLLEELRGRALAAVAAPPGAPGLVPVVHLYTDDVLVRLLPRHLGE

Ligands and cofactors

ID	Name	Formula	Copies
GPP	Geranyl diphosphate	C10 H20 O7 P2	3

Primary citation

Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5. Zhang, L., Chen, C.C., Ko, T.P. et al. Angew Chem Int Ed Engl (2016) 55:4716-4720. DOI 10.1002/anie.201511388 · PubMed

Other PDB entries of the same protein (UniProt A0A010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5B02 2.21 Å, Structure of the prenyltransferase MoeN5 with a fusion protein tag of Sso7d
6J8V 2.23 Å, Structure of MOEN5-SSO7D fusion protein in complex with ligand 2
5B0I 2.26 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-octyl glucoside
5GWW 2.3 Å, Structure of MoeN5-Sso7d fusion protein in complex with a permethylated substrate analogue
6J8W 2.35 Å, Structure of MOEN5-SSO7D fusion protein in complex with lig 1
5GWV 2.4 Å, Structure of MoeN5-Sso7d fusion protein in complex with a substrate analogue
5B0J 2.5 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-undecyl maltoside
5B03 2.6 Å, Structure of MoeN5-Sso7d fusion protein in complex with geranyl pyrophosphate
5B0K 2.75 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-decyl maltoside
5B0L 2.8 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-nonyl glucoside
5B0M 3.05 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-dodecyl maltoside
5B01 3.45 Å, Structure of a prenyltransferase in its unbound form

Browse structure collections

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