5M3Y: Human glycosylated angiotensinogen

Crystal structure of human glycosylated angiotensinogen. Determined by X-ray diffraction at 2.3 Å resolution. Released 20 Dec 2017.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,319
Mol. weight: 51.23 kDa
Released: 20 Dec 2017

Explore 5M3Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5M3Y contains 16 α-helices and 22 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, 22 β-strands

Element	Residues	Length	Sheet
β-strand	12	1	1
β-strand	33-34	2	2
α-helix	35-37	3
β-strand	38	1	3
α-helix	44-46	3
α-helix	48-60	13
α-helix	64-86	23
β-strand	96-97	2	3
β-strand	100-101	2	4
α-helix	103-115	13
α-helix	119-129	11
β-strand	142	1	1
α-helix	144-159	16
β-strand	170-180	11	3
α-helix	184-185	2
β-strand	186-187	2	2
α-helix	188-197	10
β-strand	201-205	5	3
α-helix	211-226	16
β-strand	243-254	12	3
β-strand	258-260	3	4
β-strand	265-267	3	5
β-strand	275-277	3	5
β-strand	279-291	13	4
β-strand	296-302	7	4
β-strand	307-314	8	4
α-helix	317-319	3
α-helix	320-327	8
α-helix	330-336	7
β-strand	340-349	10	4
β-strand	352-358	7	3
α-helix	359-362	4
α-helix	368-371	4
β-strand	388-400	13	3
α-helix	418	1
β-strand	419-422	4	4
β-strand	427-433	7	4
β-strand	438-445	8	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiotensinogen	A	protein	458	Homo sapiens	P01019 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5M3Y_1 Angiotensinogen (chains A)
DRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAA
KLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDH
TADRLQAILGVPWKDKQCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFT
APGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGSSLMGASVD
STLAFNTYVHFQGKMKGFSLLAEPQEFWVDQSTSVSVPMLSGMGTFQHWSDIQDQFSVTQ
VPFTESASLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQ
DLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLE
VTLNRPFLFAVYDQSATALHFLGRVANPLSTAHHHHHH

Primary citation

Structural basis for the specificity of renin-mediated angiotensinogen cleavage. Yan, Y., Zhou, A., Carrell, R.W. et al. J Biol Chem (2019) 294:2353-2364. DOI 10.1074/jbc.RA118.006608 · PubMed

Other PDB entries of the same protein (UniProt P01019 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NJ9 1.25 Å, E. coli Microcin-processing metalloprotease TldD/E with DRVY angiotensin fragment bound
5NJA 1.4 Å, E. coli Microcin-processing metalloprotease TldD/E with angiotensin analogue bound
3WOO 1.8 Å, Crystal structure of the DAP BII hexapeptide complex I
4AA1 1.99 Å, Crystal structure of ANCE in complex with Angiotensin-II
4APH 1.99 Å, Human angiotensin-converting enzyme in complex with angiotensin-II
4FYS 2.01 Å, Human aminopeptidase N (CD13) in complex with angiotensin IV
3WOR 2.1 Å, Crystal structure of the DAP BII octapeptide complex
5E2Q 2.4 Å, Structure of human DPP3 in complex with angiotensin-II
6I3F 2.55 Å, Crystal structure of the complex of human angiotensinogen and renin at 2.55 Angstrom
5M3X 2.63 Å, Crystal structure of human angiotensin I-deleted angiotensinogen
6OS0 2.9 Å, Structure of synthetic nanobody-stabilized angiotensin II type 1 receptor bound to…
6I3I 2.97 Å, Crystal structure of reactive center loop (RCL) cleaved angiotensinogen

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