5B01: Prenyltransferase in its unbound form

Name: PDB 5B01: Structure of a prenyltransferase in its unbound form
Published: 2016-11-02
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Structure of a prenyltransferase in its unbound form. Determined by X-ray diffraction at 3.45 Å resolution. Released 2 Nov 2016.

Method: X-ray diffraction
Resolution: 3.45 Å
Organism: Streptomyces ghanaensis
Chains: 10
Atoms: 20,030
Mol. weight: 322.58 kDa
Released: 2 Nov 2016

Explore 5B01 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5B01 contains 167 α-helices and 0 β-strands across 10 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 B: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	0-18	19
α-helix	23-30	8
α-helix	33-42	10
α-helix	49-74	26
α-helix	81-102	22
α-helix	107-114	8
α-helix	117-129	13
α-helix	135-142	8
α-helix	143-148	6
α-helix	149-160	12
α-helix	167-191	25
α-helix	200-205	6
α-helix	211-230	20
α-helix	236-238	3
α-helix	239-248	10
α-helix	249-253	5
α-helix	254-257	4

Chains C and I: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	0-18	19
α-helix	23-30	8
α-helix	33-42	10
α-helix	43-45	3
α-helix	49-74	26
α-helix	81-102	22
α-helix	107-114	8
α-helix	117-129	13
α-helix	135-142	8
α-helix	147-160	14
α-helix	167-191	25
α-helix	200-205	6
α-helix	211-230	20
α-helix	236-238	3
α-helix	239-248	10
α-helix	249-253	5
α-helix	254-257	4

Chain D: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	0-18	19
α-helix	23-30	8
α-helix	33-42	10
α-helix	43-45	3
α-helix	49-74	26
α-helix	81-102	22
α-helix	107-114	8
α-helix	117-129	13
α-helix	135-142	8
α-helix	147-160	14
α-helix	167-191	25
α-helix	200-205	6
α-helix	211-230	20
α-helix	238-248	11
α-helix	249-253	5
α-helix	254-257	4

Chains E, G and J: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	0-18	19
α-helix	23-30	8
α-helix	33-42	10
α-helix	43-45	3
α-helix	49-74	26
α-helix	81-102	22
α-helix	107-114	8
α-helix	117-129	13
α-helix	135-145	11
α-helix	147-160	14
α-helix	167-191	25
α-helix	200-205	6
α-helix	211-230	20
α-helix	236-238	3
α-helix	239-248	10
α-helix	249-253	5
α-helix	254-257	4

Chains F and H: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	0-18	19
α-helix	23-30	8
α-helix	33-42	10
α-helix	43-45	3
α-helix	49-74	26
α-helix	81-102	22
α-helix	107-114	8
α-helix	117-129	13
α-helix	135-145	11
α-helix	147-160	14
α-helix	167-191	25
α-helix	200-205	6
α-helix	211-230	20
α-helix	238-248	11
α-helix	249-253	5
α-helix	254-257	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MoeN5	A, B, C, D, E, F, G, H, I, J	protein	294	Streptomyces ghanaensis	A0A010 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA

>5B01_1 MoeN5 (chains A, B, C, D, E, F, G, H, I, J)
MAHHHHHHVDDDDKAASWSHPQFEKGAENLYFQSMLAAEAANRDHVTRCVAQTGGSPDLV
AHTAALRLYLRVPHFLTEWTTDPDRRAAVSRALALDIVSMKLLDDLMDDDTGLDRVELAC
VCLRLHLRALHELESLARDPKAVTDILEQDAVHLCGGQIRTKRSRATNLREWRAHASTYG
STFLGRYGALAAACGGEGQPADSVREFAEAFAMTITMADDLTDYDRNGERDGNLAHLMRT
GAVAGQDVVDLLEELRGRALAAVAAPPGAPGLVPVVHLYTDDVLVRLLPRHLGE

Primary citation

Structure and function of a prenyltransferase. Zhang, L., Chen, C.-C., Ko, T.-P. et al. To be published.

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
5B00 2.95 Å, Structure of the prenyltransferase MoeN5 in complex with geranyl pyrophosphate
5B0M 3.05 Å, Structure of MoeN5-Sso7d fusion protein in complex with beta-dodecyl maltoside

Browse structure collections

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