1HP7: Alpha-1-antitrypsin

A 2.1 Å structure of an uncleaved alpha-1-antitrypsin shows variability of the reactive center and other loops. Determined by X-ray diffraction at 2.1 Å resolution. Released 14 Mar 2001.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,089
Mol. weight: 44.74 kDa
Ligands: ZN
Released: 14 Mar 2001

Explore 1HP7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HP7 contains 13 α-helices and 17 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: 13 helices, 17 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	111-121	11	2
α-helix	128-132	5
α-helix	133-137	5
β-strand	141-145	5	2
α-helix	150-164	15
β-strand	182-191	10	2
β-strand	194	1	1
α-helix	200-202	3
β-strand	204-209	6	3
β-strand	215-227	13	3
β-strand	228-232	5	1
β-strand	237-244	8	1
β-strand	248-255	8	1
α-helix	260-266	7
α-helix	269-275	7
β-strand	282-289	8	3
β-strand	291-298	8	2
α-helix	299-305	7
α-helix	310-312	3
β-strand	331-340	10	2
β-strand	344	1	1
α-helix	361-362	2
β-strand	363-365	3	3
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

>1HP7_1 ALPHA-1-ANTITRYPSIN (chains A)
EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATA
FAMLSLGTKGDTHDEILEGLNFNLTEIPEAQIHEGFQELLHTLNQPDSQLQLTTGNGLFL
SEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDT
VFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVL
LMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLK
SVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSI
PPEVKFNKPFVFLMIDQNTKSPLFMGKVVNPTQK

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	5

Water and common crystallization additives (BME) are not listed.

Primary citation

A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops. Kim, S., Woo, J., Seo, E.J. et al. J Mol Biol (2001) 306:109-119. DOI 10.1006/jmbi.2000.4357 · 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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