6ROD: Alpha-1-antitrypsin

Alpha-1-antitrypsin (Ser36Arg/Glu78Arg/Glu266Arg) in the native conformation. Determined by X-ray diffraction at 1.85 Å resolution. Released 3 Jun 2020.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,060
Mol. weight: 45.74 kDa
Released: 3 Jun 2020

Explore 6ROD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6ROD contains 13 α-helices and 19 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, 19 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	128-136	9
β-strand	141-145	5	2
α-helix	150-164	15
β-strand	182-191	10	2
β-strand	194	1	4
α-helix	197-199	3
α-helix	200-202	3
β-strand	204-211	8	5
β-strand	214-227	14	5
β-strand	228-232	5	1
β-strand	237-243	7	1
β-strand	244	1	4
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	5
β-strand	291-298	8	2
α-helix	299-305	7
α-helix	310-312	3
β-strand	322	1	3
β-strand	331-340	10	2
β-strand	363-365	3	5
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	404	Homo sapiens	P01009 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6ROD_1 Alpha-1-antitrypsin (chains A)
MRGSHHHHHHTDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFRLYRQLAHQSNSTNI
FFSPVSIATAFAMLSLGTKADTHDEILRGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQL
QLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIV
DLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQ
HCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENRLTHDIITKFLENEDRRSASLHLPK
LSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGA
MFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK

Primary citation

Polymer accumulation in alpha-1 antitrypsin deficiency. Wan, M., Ronzoni, R., Irving, J.A. et al. To be published.

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

Browse structure collections

About this viewer

MolViewer shows 6ROD directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.