1EF0: Pi-scei miniprecursor

Crystal structure of pi-scei miniprecursor. Determined by X-ray diffraction at 2.1 Å resolution. Released 7 Jun 2000.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 6,887
Mol. weight: 103.74 kDa
Ligands: ZN
Released: 7 Jun 2000

Explore 1EF0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1EF0 contains 33 α-helices and 69 β-strands across 2 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: 17 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	1
β-strand	7-9	3	2
β-strand	10	1	3
β-strand	15-17	3	2
α-helix	18-20	3
β-strand	26-28	3	3
α-helix	29	1
β-strand	34-36	3	3
β-strand	37-39	3	4
β-strand	42-52	11	1
α-helix	67-68	2
β-strand	72-76	5	1
α-helix	79	1
β-strand	80-86	7	5
β-strand	89	1	6
β-strand	105-113	9	6
β-strand	119-127	9	6
α-helix	140-149	10
β-strand	154-160	7	5
α-helix	161-166	6
α-helix	169-174	6
β-strand	176-179	4	5
α-helix	188-195	8
α-helix	204-218	15
β-strand	219	1	7
β-strand	225-229	5	7
α-helix	233-245	13
β-strand	251-253	3	7
β-strand	261-265	5	7
α-helix	285-292	8
β-strand	296-297	2	8
β-strand	300-301	2	8
α-helix	305-309	5
α-helix	312-326	15
β-strand	327-330	4	9
β-strand	336-341	6	9
α-helix	344-356	13
β-strand	360-367	8	9
β-strand	370	1	10
β-strand	376	1	10
β-strand	379-386	8	9
α-helix	389-395	7
α-helix	406-408	3
β-strand	417-419	3	5
β-strand	421-432	12	1
β-strand	435-436	2	4
α-helix	437	1
β-strand	443-445	3	11
β-strand	446	1	2
β-strand	450	1	5
β-strand	451-453	3	11

Chain B: 16 helices, 35 β-strands

Element	Residues	Length	Sheet
β-strand	700-2	3	12
β-strand	7-9	3	13
β-strand	10	1	14
β-strand	15-17	3	13
α-helix	18-20	3
β-strand	26-28	3	14
α-helix	29	1
β-strand	34-36	3	14
β-strand	37-39	3	15
β-strand	42-52	11	12
β-strand	72-76	5	12
α-helix	79	1
β-strand	80-86	7	16
β-strand	89-93	5	17
β-strand	101-113	13	17
β-strand	119-131	13	17
α-helix	132-134	3
α-helix	137-146	10
β-strand	154-160	7	16
α-helix	161-166	6
α-helix	169-174	6
β-strand	176-179	4	16
β-strand	186	1	18
α-helix	188-192	5
α-helix	207-218	12
β-strand	225-226	2	19
β-strand	229	1	20
α-helix	233-244	12
β-strand	261	1	20
β-strand	264-265	2	19
β-strand	296-297	2	21
β-strand	300-301	2	21
α-helix	306-309	4
β-strand	310	1	18
α-helix	312-326	15
β-strand	328-330	3	22
β-strand	336-341	6	22
α-helix	344-356	13
β-strand	360-363	4	22
β-strand	381-386	6	22
α-helix	389-395	7
α-helix	406-408	3
α-helix	415-416	2
β-strand	417-419	3	16
β-strand	421-434	14	12
β-strand	435-437	3	15
β-strand	443-445	3	23
β-strand	446	1	13
β-strand	450	1	16
β-strand	451-453	3	23
β-strand	456-457	2	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Pi-scei endonuclease	A, B	protein	462	Saccharomyces cerevisiae	P17255 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1EF0_1 PI-SCEI ENDONUCLEASE (chains A, B)
KLEGAFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQH
RAHKSDSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPD
GRIVELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLSLLGSHVRKATY
QTYAPILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLM
ERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFL
KDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARS
LGLVVSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRPAPAAAFAREC
RGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVHACGER

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Structural insights into the protein splicing mechanism of PI-SceI. Poland, B.W., Xu, M.Q., Quiocho, F.A. J Biol Chem (2000) 275:16408-16413. DOI 10.1074/jbc.275.22.16408 · PubMed

Other PDB entries of the same protein (UniProt P17255 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1GPP 1.35 Å, Crystal structure of the S.cerevisiae Homing Endonuclease PI-SceI Domain I
1DFA 2.0 Å, Crystal structure of pi-scei in C2 space group
1JVA 2.1 Å, Crystal structure of the VMA1-derived endonuclease bearing the N and C extein propeptides
1VDE 2.4 Å, Pi-scei, a homing endonuclease with protein splicing activity
9COP 2.7 Å, Yeast RAVE bound to V-ATPase V1 complex
1UM2 2.9 Å, Crystal Structure of the Vma1-Derived Endonuclease with the Ligated Extein Segment
1LWT 3.2 Å, Crystal structure of the intein homing endonuclease PI-SceI bound to its substrate DNA…
7TMO 3.3 Å, V1 complex lacking subunit C from Saccharomyces cerevisiae, State 1
7TMP 3.3 Å, V1 complex lacking subunit C from Saccharomyces cerevisiae, State 2
7TMQ 3.3 Å, V1 complex lacking subunit C from Saccharomyces cerevisiae, State 3
1LWS 3.5 Å, Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition…
7TMM 3.5 Å, Complete V1 Complex from Saccharomyces cerevisiae

Browse structure collections

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