1QLP: Alpha-1-antitrypsin

2.0 Å structure of intact alpha-1-antitrypsin: a canonical template for active serpins. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Sept 1999.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 3,062
Mol. weight: 44.38 kDa
Released: 27 Sept 1999

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

Secondary structure: helices and β-sheets

1QLP contains 16 α-helices and 18 β-strands across 1 chain. 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: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	27-44	18
β-strand	50-52	3	1
α-helix	54-65	12
α-helix	70-79	10
α-helix	89-103	15
β-strand	112-121	10	2
β-strand	126	1	3
α-helix	128-132	5
α-helix	133-137	5
β-strand	141-145	5	2
α-helix	150-164	15
β-strand	182-190	9	2
β-strand	194	1	1
α-helix	197-199	3
α-helix	200-202	3
β-strand	204-209	6	4
β-strand	215-227	13	4
β-strand	228-232	5	1
β-strand	237-244	8	1
β-strand	248-255	8	1
α-helix	256	1
α-helix	260-266	7
α-helix	269-277	9
β-strand	282-289	8	4
β-strand	291-298	8	2
α-helix	299-302	4
α-helix	304-306	3
α-helix	310-312	3
β-strand	322	1	3
β-strand	331-340	10	2
α-helix	348-351	4
β-strand	363-365	3	4
β-strand	370-376	7	1
β-strand	382-388	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-1-antitrypsin	A	protein	394	HOMO SAPIENS	P01009 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1QLP_1 ALPHA-1-ANTITRYPSIN (chains A)
MDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATA
FAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFL
SEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDT
VFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVL
LMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLK
SVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSI
PPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK

Primary citation

Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets for rational drug design to prevent conformational disease. Elliott, P.R., Pei, X.Y., Dafforn, T.R. et al. Protein Sci (2000) 9:1274-1281. DOI 10.1110/ps.9.7.1274 · PubMed

Other PDB entries of the same protein (UniProt P01009 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8PI2 1.48 Å, Native alpha-1-antitrypsin at 1.5 Angstrom (Cys232Ser)
3NDD 1.5 Å, Cleaved antitrypsin with P10 Pro, and P9-P6 Asp
6I7U 1.55 Å, Alpha-1-antitrypsin (Ala250Met) in the native conformation
5NBU 1.67 Å, Crystal structure of native alpha-1-antitrypsin with seven stabilising mutations
8QZ5 1.69 Å, Alpha-1-antitrypsin (Tyr244Phe) in the native conformation
5NBV 1.73 Å, Crystal structure of native alpha-1-antitrypsin with seven stabilising mutations
7AEL 1.76 Å, alpha 1-antitrypsin (C232S) complexed with GSK716
6I4V 1.78 Å, Alpha-1-antitrypsin Queen's (K154N) variant
3NE4 1.81 Å, 1.8 Angstrom structure of intact native wild-type alpha-1-antitrypsin
7NPL 1.82 Å, Alpha-1 antitrypsin (C232S) complexed with cmpd 11
7NPK 1.83 Å, Alpha-1 antitrypsin C232S complexed with CMPD3
9GGP 1.84 Å, Alpha-1-antitrypsin in complex with the Fab fragment of an anti-polymer antibody

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