4XAI: Red flour beetle NR2E1/TLX

Crystal Structure of red flour beetle NR2E1/TLX. Determined by X-ray diffraction at 2.6 Å resolution. Released 4 Mar 2015.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Escherichia coli O157:H7, Tribolium castaneum, Drosophila melanogaster
Chains: 4
Atoms: 9,306
Mol. weight: 132.78 kDa
Released: 4 Mar 2015

Explore 4XAI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4XAI contains 77 α-helices and 50 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: 38 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	4-5	2
β-strand	9-12	4	1
α-helix	19-33	15
β-strand	37-40	4	1
α-helix	45-52	8
α-helix	53-55	3
β-strand	61-65	5	1
α-helix	66-68	3
α-helix	69-74	6
β-strand	78	1	2
α-helix	79-81	3
α-helix	85-88	4
β-strand	91	1	3
α-helix	93-98	6
β-strand	100-101	2	4
β-strand	104-105	2	4
β-strand	108-113	6	1
β-strand	116-120	5	5
β-strand	130	1	6
α-helix	134-141	8
β-strand	147-149	3	5
α-helix	156-163	8
β-strand	169	1	7
β-strand	172-173	2	8
β-strand	178-179	2	8
β-strand	184	1	7
α-helix	188-202	15
α-helix	212-221	10
β-strand	224-229	6	5
α-helix	231-233	3
α-helix	234-240	7
β-strand	244-247	4	5
α-helix	248-250	3
β-strand	251	1	6
β-strand	252	1	9
β-strand	255	1	9
α-helix	256-257	2
β-strand	260-261	2	10
β-strand	262-268	7	1
β-strand	269	1	2
α-helix	275-281	7
α-helix	282-286	5
α-helix	289-296	8
β-strand	303-304	2	1
β-strand	306	1	3
α-helix	307-313	7
α-helix	317-327	11
β-strand	330-331	2	10
α-helix	332-333	2
α-helix	338-354	17
α-helix	359-370	12
α-helix	372-374	3
α-helix	1196-1216	21
α-helix	1218-1221	4
α-helix	1225-1247	23
α-helix	1254-1255	2
α-helix	1256-1261	6
α-helix	1272-1290	19
α-helix	1294-1305	12
α-helix	1326-1347	22
α-helix	1354-1367	14
α-helix	1371-1374	4
α-helix	1375-1379	5
α-helix	1386-1395	10

Chain B: 37 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	4-5	2
β-strand	9-12	4	11
α-helix	19-33	15
β-strand	37-40	4	11
α-helix	45-52	8
β-strand	61-65	5	11
α-helix	66-68	3
α-helix	69-74	6
β-strand	78	1	12
α-helix	79-81	3
α-helix	85-88	4
β-strand	91	1	13
α-helix	93-98	6
β-strand	100-101	2	14
β-strand	104-105	2	14
β-strand	107-113	7	11
β-strand	116-120	5	15
β-strand	130	1	16
α-helix	134-141	8
α-helix	142-144	3
β-strand	147-149	3	15
α-helix	156-165	10
β-strand	171-174	4	17
β-strand	177-183	7	17
α-helix	188-202	15
α-helix	212-220	9
β-strand	224-229	6	15
α-helix	231-233	3
α-helix	234-238	5
β-strand	244-247	4	15
α-helix	248-250	3
β-strand	251	1	16
β-strand	252	1	18
β-strand	255	1	18
α-helix	256-257	2
α-helix	259	1
β-strand	260-261	2	19
β-strand	262-268	7	11
β-strand	269	1	12
α-helix	275-281	7
α-helix	282-286	5
α-helix	289-296	8
β-strand	303-304	2	11
β-strand	306	1	13
α-helix	307-313	7
α-helix	317-328	12
β-strand	330-331	2	19
α-helix	332-333	2
α-helix	338-353	16
α-helix	362-1215	33
α-helix	1218-1221	4
α-helix	1225-1247	23
α-helix	1253-1256	4
α-helix	1257-1261	5
α-helix	1263-1265	3
α-helix	1272-1289	18
α-helix	1294-1305	12
α-helix	1326-1347	22
α-helix	1354-1366	13
α-helix	1371-1377	7
α-helix	1387-1394	8

Chains P and Q: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1818-1825	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose-binding periplasmic protein,Tailless ortholog	A, B	protein	573	Escherichia coli O157:H7, Tribolium castaneum	P0AEY0 (AlphaFold model), Q9NCL0 (AlphaFold model)
Grunge, isoform J	P, Q	protein	21	Drosophila melanogaster	M9PHT1 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4XAI_1 Maltose-binding periplasmic protein,Tailless ortholog (chains A, B)
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII
FWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD
LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD
VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEA
LKDAQTNAAAEFPSAICESAAQLIFMNVQWVRSIPAFTCLPLSDQLLLLEESWLDLFVLG
AAQFLPLMDFSVLVEACGVLQQEPHRRDAFLKEVADFQETLKKISQFQLDAHEFACLRAI
VLFKTSFEKPSSSSNQEKTTTESAKISVIQDDAQMRLNKHVTTTYPKQPLRFGKILLLVS
STFRTISGRTIEDLFFKKVIRDTPIVAIISNMY

Sequence of entity 2 (P, Q), FASTA

>4XAI_2 Grunge, isoform J (chains P, Q)
YADTPALRQLSEYARPHVAFS

Primary citation

Structural basis for corepressor assembly by the orphan nuclear receptor TLX. Zhi, X., Zhou, X.E., He, Y. et al. Genes Dev (2015) 29:440-450. DOI 10.1101/gad.254904.114 · PubMed

Other PDB entries of the same protein (UniProt P0AEY0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9PQP 1.07 Å, Crystal structure of maltose binding protein (Apo), mutant Trp340 to 4-Fluorotryptophan
9PQL 1.37 Å, Crystal structure of maltose binding protein (Apo), mutant Trp62 to 4-Fluorotryptophan
9PQN 1.37 Å, Crystal structure of maltose binding protein (Apo), mutant Trp340 to 4-Cyanotryptophan
9TY2 1.75 Å, Crystal structure of a Picomolar Nanobody in complex with Maltose Binding Protein, MBP,…
4WGI 1.85 Å, A Single Diastereomer of a Macrolactam Core Binds Specifically to Myeloid Cell Leukemia…
9PQK 1.87 Å, Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Fluorotryptophan
4WVI 1.9 Å, Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB) in…
4WVJ 1.95 Å, Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB) in…
4YS9 2.0 Å, Ataxin-3 Carboxy-Terminal Region - Crystal C1 (tetragonal)
5II4 2.0 Å, Crystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution
5JON 2.04 Å, Crystal structure of the unliganded form of HCN2 CNBD
4WVG 2.05 Å, Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB).

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