5M3X: Human angiotensin I-deleted angiotensinogen

Crystal structure of human angiotensin I-deleted angiotensinogen. Determined by X-ray diffraction at 2.63 Å resolution. Released 20 Dec 2017.

Method
X-ray diffraction
Resolution
2.63 Å
Organism
Homo sapiens
Chains
2
Atoms
5,923
Mol. weight
98.73 kDa
Released
20 Dec 2017

Explore 5M3X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5M3X contains 34 α-helices and 40 β-strands across 2 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 A: 17 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand33-3421
α-helix35-362
β-strand37-3822
α-helix44-463
α-helix48-6013
α-helix64-8623
α-helix91-944
β-strand96-9722
β-strand99-10133
α-helix103-11513
α-helix119-12911
α-helix133-1353
α-helix144-15916
β-strand170-180112
α-helix184-1852
β-strand186-18721
α-helix188-19710
β-strand200-20562
α-helix211-22616
β-strand243-254122
β-strand258-26033
β-strand265-26734
β-strand275-27734
β-strand279-291133
β-strand296-30273
β-strand307-31483
α-helix317-3193
α-helix320-3278
β-strand340-349103
β-strand351-35882
α-helix359-3624
α-helix364-3663
α-helix368-3714
β-strand388-400132
β-strand419-42243
β-strand427-43373
β-strand438-44583
Chain B: 17 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand33-3425
α-helix35-373
β-strand3816
α-helix44-463
α-helix48-6013
α-helix64-8623
α-helix91-933
β-strand96-9726
β-strand99-10137
α-helix103-11513
α-helix119-12911
α-helix134-1363
α-helix144-15916
β-strand170-180116
α-helix184-1852
β-strand186-18725
α-helix188-19710
β-strand200-20566
α-helix211-22616
β-strand243-254126
β-strand258-26037
β-strand265-26738
β-strand275-27738
β-strand279-291137
β-strand296-30277
β-strand307-31487
α-helix317-3193
α-helix320-3278
β-strand340-349107
β-strand351-35886
α-helix359-3624
α-helix364-3663
α-helix368-3736
β-strand388-400136
β-strand419-42247
β-strand427-43377
β-strand438-44587

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AngiotensinogenA, Bprotein448Homo sapiensP01019 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5M3X_1 Angiotensinogen (chains A, B)
VIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRA
AMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILG
VPWKDKQCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPF
VQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGSSLMGASVDSTLAFNTYVH
FQGKMKGFSLLAEPQEFWVDQSTSVSVPMLSGMGTFQHWSDIQDQFSVTQVPFTESASLL
LIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPA
ILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFA
VYDQSATALHFLGRVANPLSTAHHHHHH

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:

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