5HZJ: Intersectin-1,NPH1-1,Intersectin-1

Crystal structure of photoinhibitable Intersectin1 containing wildtype LOV2 domain. Determined by X-ray diffraction at 2.6 Å resolution. Released 21 Dec 2016.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Homo sapiens, Avena sativa
Chains: 2
Atoms: 7,915
Mol. weight: 117.47 kDa
Ligands: FMN
Released: 21 Dec 2016

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

Secondary structure: helices and β-sheets

5HZJ contains 42 α-helices and 34 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: 21 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	1233-1259	27
α-helix	1260-1264	5
α-helix	1265-1269	5
α-helix	1275-1282	8
α-helix	1285-1302	18
α-helix	1308-1314	7
β-strand	1320-1323	4	1
β-strand	1332-1335	4	1
α-helix	1337-1343	7
α-helix	1347-1350	4
α-helix	1355-1358	4
β-strand	1359	1	1
α-helix	1365-1376	12
β-strand	1381-1388	8	1
β-strand	1394-1405	12	1
β-strand	1411-1421	11	1
α-helix	1427-1447	21
α-helix	1459-1465	7
α-helix	1466-1468	3
α-helix	1471-1477	7
α-helix	1479-1491	13
α-helix	1494-1501	8
α-helix	1514-1516	3
α-helix	1520-1537	18
α-helix	1546-1568	23
α-helix	1570-1582	13
β-strand	1583-1584	2	2
β-strand	1597	1	3
β-strand	1603	1	3
β-strand	1606-1614	9	2
β-strand	1620-1626	7	2
β-strand	1629-1635	7	2
β-strand	1656-1658	3	2
β-strand	1663-1664	2	2
β-strand	1668-1671	4	2
β-strand	1682-1687	6	2
β-strand	1691-1695	5	2
α-helix	1699-1720	22

Chain B: 21 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	1233-1259	27
α-helix	1260-1264	5
α-helix	1265-1270	6
α-helix	1275-1281	7
α-helix	1285-1302	18
α-helix	1308-1314	7
β-strand	1320-1323	4	4
β-strand	1332-1335	4	4
α-helix	1337-1343	7
α-helix	1347-1350	4
α-helix	1355-1358	4
β-strand	1359	1	4
α-helix	1365-1376	12
β-strand	1381-1388	8	4
β-strand	1394-1405	12	4
β-strand	1411-1421	11	4
α-helix	1427-1447	21
α-helix	1459-1465	7
α-helix	1466-1468	3
α-helix	1471-1491	21
α-helix	1494-1501	8
α-helix	1514-1517	4
α-helix	1520-1525	6
α-helix	1527-1537	11
α-helix	1546-1568	23
α-helix	1570-1582	13
β-strand	1583-1584	2	5
β-strand	1597	1	6
β-strand	1603	1	6
β-strand	1606-1614	9	5
β-strand	1620-1626	7	5
β-strand	1629-1635	7	5
β-strand	1656-1658	3	5
β-strand	1663-1664	2	5
β-strand	1668-1671	4	5
β-strand	1682-1687	6	5
β-strand	1691-1695	5	5
α-helix	1699-1720	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Intersectin-1,NPH1-1,Intersectin-1	A, B	protein	502	Homo sapiens, Avena sativa	O49003 (AlphaFold model), Q15811 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5HZJ_1 Intersectin-1,NPH1-1,Intersectin-1 (chains A, B)
MLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLMESELLTEKEVAMIFVNWKELI
MCNIKLLKALRVRKKMSGELATTLERIEKNFVITDPRLPDNPIIFASDSFLQLTEYSREE
ILGRNCRFLQGPETDRATVRKIRDAIDNQTEVTVQLINYTKSGKKFWNLFHLQPMRDQKG
DVQYFIGVQLDGTEHVRDAAEREGVMLIKKTAENIDEAAKELKMPVKMIGDILSAQLPHM
QPYIRFCSRQLNGAALIQQKTDEAPDFKEFVKRLAMDPRCKGMPLSSFILKPMQRVTRYP
LIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLS
EQLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFS
PKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKI
KAASELYIETEKKKLEHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
FMN	Flavin mononucleotide	C17 H21 N4 O9 P	2

Primary citation

Engineering extrinsic disorder to control protein activity in living cells. Dagliyan, O., Tarnawski, M., Chu, P.H. et al. Science (2016) 354:1441-1444. DOI 10.1126/science.aah3404 · PubMed

Other PDB entries of the same protein (UniProt O49003 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7PGZ 0.9 Å, Structure of dark-adapted AsLOV2 Q513L
7PH0 0.98 Å, Structure of light-adapted AsLOV2 Q513L
7PGX 1.0 Å, Structure of dark-adapted AsLOV2 wild type
7PGY 1.09 Å, Structure of light-adapted AsLOV2 wild type
2V0U 1.4 Å, n- and c-terminal helices of oat lov2 (404-546) are involved in light-induced signal…
2V1B 1.55 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal…
2WKQ 1.6 Å, Structure of a photoactivatable Rac1 containing the Lov2 C450A Mutant
2V1A 1.65 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal…
2V0W 1.7 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light- induced signal…
6NTP 1.89 Å, PTP1B Domain of PTP1B-LOV2 Chimera
2WKP 1.9 Å, Structure of a photoactivatable Rac1 containing Lov2 Wildtype
4WF0 1.95 Å, Crystal Structure of iLID - an Improved Light-Inducible Dimer

Browse structure collections

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