1AL0: Procapsid of bacteriophage PHIX174

Procapsid of bacteriophage PHIX174. Determined by X-ray diffraction at 3.5 Å resolution. Released 28 Jan 1998.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Enterobacteria phage phiX174
Chains: 7
Atoms: 9,521
Mol. weight: 149.16 kDa
Released: 28 Jan 1998

Explore 1AL0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1AL0 contains 63 α-helices and 56 β-strands across 7 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 1: 13 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	7-22	16
α-helix	31-37	7
α-helix	45-47	3
α-helix	48-59	12
α-helix	61-66	6
α-helix	68-70	3
α-helix	72-74	3
α-helix	75-85	11
α-helix	92-96	5
β-strand	100	1	1
α-helix	101-103	3
α-helix	104-109	6
β-strand	115	1	1
α-helix	117-129	13
α-helix	140-143	4

Chain 2: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	12-24	13
α-helix	31-38	8
α-helix	45-47	3
α-helix	48-66	19
β-strand	73	1	2
α-helix	75-84	10
α-helix	88-90	3
α-helix	91-98	8
β-strand	104	1	2
β-strand	106-107	2	3
β-strand	112-113	2	3
α-helix	114-116	3
α-helix	119-127	9

Chain 3: 9 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-23	14
α-helix	31-38	8
α-helix	45-47	3
α-helix	48-65	18
α-helix	75-85	11
α-helix	88-90	3
α-helix	91-97	7
β-strand	102	1	4
α-helix	104-109	6
β-strand	114	1	4
α-helix	117-130	14

Chain 4: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	11-20	10
α-helix	31-37	7
α-helix	42-43	2
α-helix	48-65	18
α-helix	75-84	10
α-helix	91-98	8
α-helix	117-128	12
α-helix	133-148	16

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	87-90	4
α-helix	101-102	2
α-helix	112-115	4

Chain F: 18 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	10-13	4	5
β-strand	16-22	7	5
β-strand	26-27	2	6
β-strand	28	1	7
β-strand	32-35	4	8
β-strand	42-49	8	5
β-strand	62-66	5	7
β-strand	69-72	4	8
α-helix	73-75	3
α-helix	81-87	7
α-helix	88-90	3
β-strand	96-98	3	9
α-helix	107-109	3
β-strand	118-120	3	9
α-helix	121-134	14
α-helix	141-142	2
α-helix	148-150	3
α-helix	153-157	5
α-helix	159	1
β-strand	160-161	2	6
β-strand	163	1	10
β-strand	186	1	11
β-strand	189	1	11
α-helix	192-210	19
α-helix	215-220	6
β-strand	235	1	8
β-strand	240-244	5	7
β-strand	250	1	12
β-strand	260	1	12
β-strand	267-272	6	5
β-strand	281-284	4	8
β-strand	287-290	4	7
α-helix	291-293	3
β-strand	298	1	13
α-helix	301-304	4
α-helix	310-313	4
α-helix	317-321	5
β-strand	326-329	4	14
α-helix	330-332	3
β-strand	334	1	13
β-strand	342-345	4	14
α-helix	349-351	3
β-strand	363	1	15
β-strand	365	1	15
β-strand	384	1	10
α-helix	391-393	3
β-strand	402-414	13	5

Chain G: 2 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	15-17	3	16
β-strand	22-23	2	16
β-strand	26	1	17
β-strand	30	1	18
β-strand	31	1	17
β-strand	36	1	17
β-strand	39-49	11	16
α-helix	50	1
β-strand	52-61	10	17
β-strand	70-73	4	19
β-strand	76-81	6	16
β-strand	88-96	9	17
β-strand	102	1	18
β-strand	108-110	3	17
β-strand	115-117	3	16
β-strand	120-124	5	16
β-strand	127-130	4	19
β-strand	139-150	12	17
β-strand	153-162	10	16
β-strand	163-164	2	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Scaffolding protein gpd	1, 2, 3, 4	protein	152	Enterobacteria phage phiX174	P69486
Capsid protein gpf	F	protein	426	Enterobacteria phage phiX174	P03641
Spike protein gpg	G	protein	175	Enterobacteria phage phiX174	P03643
Scaffolding protein gpb	B	protein	120	Enterobacteria phage phiX174	P03633

Sequence of entity 1 (1, 2, 3, 4), FASTA

>1AL0_1 SCAFFOLDING PROTEIN GPD (chains 1, 2, 3, 4)
MSQVTEQSVRFQTALASIKLIQASAVLDLTEDDFDFLTSNKVWIATDRSRARRCVEACVY
GTLDFVGYPRFPAPVEFIAAVIAYYVHPVNIQTACLIMEGAEFTENIINGVERPVKAAEL
FAFTLRVRAGNTDVLTDAEENVRQKLRAEGVM

Sequence of entity 2 (F), FASTA

>1AL0_2 CAPSID PROTEIN GPF (chains F)
SNIQTGAERMPHDLSHLGFLAGQIGRLITISTTPVIAGDSFEMDAVGALRLSPLRRGLAI
DSTVDIFTFYVPHRHVYGEQWIKFMKDGVNATPLPTVNTTGYIDHAAFLGTINPDTNKIP
KHLFQGYLNIYNNYFKAPWMPDRTEANPNELNQDDARYGFRCCHLKNIWTAPLPPETELS
RQMTTSTTSIDIMGLQAAYANLHTDQERDYFMQRYRDVISSFGGKTSYDADNRPLLVMRS
NLWASGYDVDGTDQTSLGQFSGRVQQTYKHSVPRFFVPEHGTMFTLALVRFPPTATKEIQ
YLNAKGALTYTDIAGDPVLYGNLPPREISMKDVFRSGDSSKKFKIAEGQWYRYAPSYVSP
AYHLLEGFPFIQEPPSGDLQERVLIRHHDYDQCFQSVQLLQWNSQVKFNVTVYRNLPTTR
DSIMTS

Sequence of entity 3 (G), FASTA

>1AL0_3 SPIKE PROTEIN GPG (chains G)
MFQTFISRHNSNFFSDKLVLTSVTPASSAPVLQTPKATSSTLYFDSLTVNAGNGGFLHCI
QMDTSVNAANQVVSVGADIAFDADPKFFACLVRFESSSVPTTLPTAYDVYPLNGRHDGGY
YTVKDCVTIDVLPRTPGNNVYVGFMVWSNFTATKCRGLVSLNQVIKEIICLQPLK

Sequence of entity 4 (B), FASTA

>1AL0_4 SCAFFOLDING PROTEIN GPB (chains B)
MEQLTKNQAVATSQEAVQNQNEPQLRDENAHNDKSVHGVLNPTYQAGLRRDAVQPDIEAE
RKKRDEIEAGKSYCSRRFGGATCDDKSAQIYARFDKNDWRIQPAEFYRFHDAEVNTFGYF

Primary citation

Structure of a viral procapsid with molecular scaffolding. Dokland, T., McKenna, R., Ilag, L.L. et al. Nature (1997) 389:308-313. DOI 10.1038/38537 · PubMed

Other PDB entries of the same protein (UniProt P69486), best resolution first:

1TX9 3.31 Å, gpd prior to capsid assembly
1CD3 3.5 Å, Procapsid of bacteriophage PHIX174
1M0F 16.0 Å, Structural Studies of Bacteriophage alpha3 Assembly, Cryo-electron microscopy

Browse structure collections

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