3BG0: Protein SEC13 homolog

Architecture of a Coat for the Nuclear Pore Membrane. Determined by X-ray diffraction at 3.15 Å resolution. Released 1 Jan 2008.

Method: X-ray diffraction
Resolution: 3.15 Å
Organisms: Homo sapiens, Saccharomyces cerevisiae
Chains: 8
Atoms: 22,562
Mol. weight: 343.35 kDa
Released: 1 Jan 2008

Explore 3BG0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BG0 contains 116 α-helices and 144 β-strands across 8 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: 3 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	1
β-strand	27-32	6	1
β-strand	36-41	6	1
β-strand	52-54	3	1
β-strand	60-65	6	2
α-helix	66-67	2
β-strand	69	1	3
β-strand	71	1	3
β-strand	74-78	5	2
β-strand	83-86	4	2
β-strand	95-99	5	2
β-strand	106-111	6	4
α-helix	114-116	3
β-strand	120-124	5	4
β-strand	129-134	6	4
β-strand	140-142	3	4
β-strand	153	1	5
β-strand	157-158	2	6
α-helix	159-160	2
β-strand	181	1	7
β-strand	182-183	2	6
β-strand	185	1	8
β-strand	186	1	5
β-strand	191	1	8
β-strand	193-196	4	7
β-strand	202-206	5	7
β-strand	215-219	5	9
β-strand	230-235	6	9
β-strand	239-244	6	9
β-strand	257-260	4	9
β-strand	265-270	6	10
β-strand	277-281	5	10
β-strand	286-291	6	10
β-strand	297-302	6	10

Chain B: 26 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	138-141	4
β-strand	151	1	11
β-strand	161	1	11
α-helix	173-177	5
α-helix	182-185	4
α-helix	187-195	9
β-strand	197-201	5	12
β-strand	208-213	6	12
α-helix	217-221	5
α-helix	229-240	12
α-helix	243-244	2
α-helix	253-272	20
α-helix	277-281	5
α-helix	290-299	10
α-helix	303-312	10
α-helix	316-324	9
α-helix	330-342	13
α-helix	352-362	11
α-helix	373-377	5
α-helix	381-390	10
α-helix	399-409	11
α-helix	417-426	10
α-helix	431-438	8
α-helix	447-458	12
α-helix	467-483	17
α-helix	487-494	8
α-helix	500-514	15
α-helix	516-518	3
α-helix	526-529	4
α-helix	534-551	18

Chain C: 25 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	133-142	10
β-strand	152-153	2	13
β-strand	158-162	5	13
β-strand	170-174	5	13
α-helix	175-176	2
α-helix	182-185	4
α-helix	187-195	9
β-strand	197-201	5	14
β-strand	208-213	6	14
α-helix	218-221	4
α-helix	229-240	12
α-helix	253-272	20
α-helix	277-281	5
α-helix	290-299	10
α-helix	303-312	10
α-helix	316-324	9
α-helix	330-342	13
α-helix	352-362	11
α-helix	373-377	5
α-helix	381-390	10
α-helix	399-409	11
α-helix	417-426	10
α-helix	431-438	8
α-helix	447-458	12
α-helix	467-483	17
α-helix	487-495	9
α-helix	500-514	15
α-helix	516-518	3
α-helix	526-529	4
α-helix	534-551	18

Chain D: 3 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	15
β-strand	27-32	6	15
β-strand	36-41	6	15
β-strand	51-54	4	15
β-strand	60-65	6	16
α-helix	66-67	2
β-strand	69	1	17
β-strand	71	1	17
β-strand	74-78	5	16
β-strand	83-86	4	16
β-strand	95-99	5	16
β-strand	106-111	6	18
α-helix	114-116	3
β-strand	120-124	5	18
β-strand	129-134	6	18
β-strand	140-142	3	18
β-strand	153	1	19
β-strand	157-158	2	20
α-helix	159-160	2
β-strand	182-183	2	20
β-strand	185	1	21
β-strand	186	1	19
β-strand	191	1	21
β-strand	193	1	22
β-strand	206	1	22
β-strand	215-219	5	23
β-strand	232-235	4	23
β-strand	239-244	6	23
β-strand	254-260	7	23
β-strand	265-270	6	24
β-strand	276-281	6	24
β-strand	286-291	6	24
β-strand	297-299	3	24

Chain E: 3 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	25
β-strand	27-32	6	25
β-strand	36-41	6	25
β-strand	51-54	4	25
β-strand	60-65	6	26
α-helix	66-67	2
β-strand	69	1	27
β-strand	71	1	27
β-strand	74-78	5	26
β-strand	83-86	4	26
β-strand	95-99	5	26
β-strand	106-111	6	28
α-helix	114-116	3
β-strand	120-124	5	28
β-strand	129-134	6	28
β-strand	140-142	3	28
β-strand	153	1	29
β-strand	157-158	2	30
α-helix	159-160	2
β-strand	181	1	31
β-strand	182-183	2	30
β-strand	185	1	32
β-strand	186	1	29
β-strand	191	1	32
β-strand	193-196	4	31
β-strand	202-206	5	31
β-strand	215-219	5	33
β-strand	230-235	6	33
β-strand	239-245	7	33
β-strand	253-254	2	33
β-strand	257-260	4	33
β-strand	265-270	6	34
β-strand	277-281	5	34
β-strand	286-291	6	34
β-strand	297-302	6	34

Chain F: 26 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	138-141	4
β-strand	151	1	35
β-strand	161	1	35
α-helix	173-177	5
α-helix	182-185	4
α-helix	187-195	9
β-strand	197-201	5	36
β-strand	208-213	6	36
α-helix	217-221	5
α-helix	229-240	12
α-helix	243-244	2
α-helix	253-272	20
α-helix	277-281	5
α-helix	290-299	10
α-helix	303-312	10
α-helix	316-324	9
α-helix	330-342	13
α-helix	352-362	11
α-helix	373-377	5
α-helix	381-390	10
α-helix	399-409	11
α-helix	417-426	10
α-helix	431-438	8
α-helix	447-458	12
α-helix	467-483	17
α-helix	489-494	6
α-helix	500-514	15
α-helix	516-518	3
α-helix	526-529	4
α-helix	534-551	18

Chain G: 27 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	133-142	10
β-strand	152-153	2	37
β-strand	158-162	5	37
β-strand	170-174	5	37
α-helix	175-176	2
α-helix	182-185	4
α-helix	187-195	9
β-strand	197-201	5	38
β-strand	208-213	6	38
α-helix	217-221	5
α-helix	229-240	12
α-helix	243-244	2
α-helix	253-272	20
α-helix	277-281	5
α-helix	290-299	10
α-helix	303-312	10
α-helix	316-324	9
α-helix	330-342	13
α-helix	352-362	11
α-helix	373-377	5
α-helix	381-390	10
α-helix	399-409	11
α-helix	411-413	3
α-helix	417-426	10
α-helix	431-438	8
α-helix	447-458	12
α-helix	467-483	17
α-helix	487-495	9
α-helix	500-514	15
α-helix	516-518	3
α-helix	526-529	4
α-helix	534-551	18

Chain H: 3 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	39
β-strand	27-32	6	39
β-strand	36-41	6	39
β-strand	51-54	4	39
β-strand	60-65	6	40
α-helix	66-67	2
β-strand	69	1	41
β-strand	71	1	41
β-strand	74-78	5	40
β-strand	83-86	4	40
β-strand	95-99	5	40
β-strand	106-111	6	42
α-helix	114-116	3
β-strand	120-124	5	42
β-strand	129-134	6	42
β-strand	140-142	3	42
β-strand	153	1	43
β-strand	157-158	2	44
α-helix	159-160	2
β-strand	181	1	45
β-strand	182-183	2	44
β-strand	185	1	46
β-strand	186	1	43
β-strand	191	1	46
β-strand	193-197	5	45
β-strand	201-206	6	45
β-strand	215-219	5	47
β-strand	232-235	4	47
β-strand	239-242	4	47
β-strand	244-245	2	48
β-strand	253-254	2	48
β-strand	257-260	4	47
β-strand	265-270	6	49
β-strand	277-281	5	49
β-strand	286-292	7	49
β-strand	296-299	4	49

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein SEC13 homolog	A, D, E, H	protein	316	Homo sapiens	P55735 (AlphaFold model)
Nucleoporin NUP145	B, C, F, G	protein	442	Saccharomyces cerevisiae	P49687 (AlphaFold model)

Sequence of entity 1 (A, D, E, H), FASTA

>3BG0_1 Protein SEC13 homolog (chains A, D, E, H)
MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPV
WQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLIL
ACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDHPSGQKPNYIK
RFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRV
FIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCI
SDVNKGQGSVSASVTE

Sequence of entity 2 (B, C, F, G), FASTA

>3BG0_2 Nucleoporin NUP145 (chains B, C, F, G)
MGSSHHHHHHSGDPFSECNDEIDNAKLIMKERRFTASYTFAKFSTGSMLLTKDIVGKSGV
SIKRLPTELQRKFLFDDVYLDKEIEKVTIEARKSNPYPQISESSLLFKDALDYMEKTSSD
YNLWKLSSILFDPVSYPYKTDNDQVKMALLKKERHCRLTSWIVSQIGPEIEEKIRNSSNE
IEQIFLYLLLNDVVRASKLAIESKNGHLSVLISYLGSNDPRIRDLAELQLQKWSTGGCSI
DKNISKIYKLLSGSPFEGLFSLKELESEFSWLCLLNLTLCYGQIDEYSLESLVQSHLDKF
SLPYDDPIGVIFQLYAANENTEKLYKEVRQRTNALDVQFCWYLIQTLRFNGTRVFSKETS
DEATFAFAAQLEFAQLHGHSLFVSCFLNDDKAAEDTIKRLVMREITLLRASTNDHILNRL
KIPSQLIFNAQALKDRYEGNYL

Primary citation

Architecture of a coat for the nuclear pore membrane. Hsia, K.C., Stavropoulos, P., Blobel, G. et al. Cell (2007) 131:1313-1326. DOI 10.1016/j.cell.2007.11.038 · PubMed

Other PDB entries of the same protein (UniProt P55735 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3BG1 3.0 Å, Architecture of a Coat for the Nuclear Pore Membrane
9DX1 3.36 Å, Human GATOR2 complex - Sestrin2 bound state
9DX2 3.4 Å, Human GATOR2 complex - CASTOR1 bound state
9LWF 3.41 Å, Cryo-EM structure of dual sensor bound GATOR2 complex
9DX0 3.47 Å, Human GATOR2 complex - apo state
9OTI 3.5 Å, GATOR2 complex bound to arginine sensor CASTOR1
9LVK 3.59 Å, Cryo-EM structure of CASTOR1 bound human GATOR2 complex
7UHY 3.66 Å, Human GATOR2 complex
9LVJ 3.82 Å, Cryo-EM structure of Sestrin2 bound human GATOR2 complex
7R5K 12.0 Å, Human nuclear pore complex (constricted)
5A9Q 23.0 Å, Human nuclear pore complex
7PEQ 35.0 Å, Model of the outer rings of the human nuclear pore complex

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