2X0B: Human angiotensinogen

Crystal structure of human angiotensinogen complexed with renin. Determined by X-ray diffraction at 4.33 Å resolution. Released 20 Oct 2010.

Method: X-ray diffraction
Resolution: 4.33 Å
Organism: HOMO SAPIENS
Chains: 8
Atoms: 23,244
Mol. weight: 368.69 kDa
Released: 20 Oct 2010

Explore 2X0B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2X0B contains 124 α-helices and 223 β-strands across 8 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.

Chains A, C, E and G: 15 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	8-10	3	2
β-strand	14-21	8	2
β-strand	26-33	8	2
β-strand	39-42	4	2
β-strand	43	1	3
α-helix	51-54	4
β-strand	59	1	3
α-helix	61-63	3
β-strand	68-77	10	2
β-strand	82-94	13	2
β-strand	97-108	12	2
α-helix	111-114	4
β-strand	121-124	4	2
α-helix	128-130	3
α-helix	132-134	3
α-helix	135-137	3
α-helix	138-143	6
β-strand	152-157	6	1
β-strand	167-171	5	1
α-helix	176-178	3
β-strand	179-187	9	1
β-strand	188	1	4
β-strand	195-198	4	4
β-strand	200-203	4	5
β-strand	209	1	5
β-strand	214-218	5	4
β-strand	225-227	3	4
α-helix	229-239	11
α-helix	241	1
β-strand	242-243	2	6
β-strand	248-251	4	6
α-helix	252-254	3
α-helix	258-260	3
β-strand	261-265	5	5
β-strand	268-272	5	5
α-helix	274-277	4
β-strand	278	1	7
β-strand	288-290	3	6
β-strand	291	1	7
β-strand	293-295	3	4
α-helix	298-299	2
β-strand	306-308	3	4
α-helix	310-313	4
β-strand	316-321	6	1
β-strand	326-332	7	1

Chain B: 16 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	33-34	2	8
α-helix	35-37	3
β-strand	38	1	9
α-helix	43-46	4
α-helix	48-60	13
α-helix	64-84	21
α-helix	85-87	3
β-strand	97	1	10
β-strand	100-101	2	11
α-helix	103-115	13
α-helix	121-129	9
α-helix	145-158	14
β-strand	170-179	10	10
α-helix	180-181	2
β-strand	186-187	2	8
α-helix	188-197	10
β-strand	201-203	3	10
β-strand	205	1	9
α-helix	211-226	16
β-strand	244-255	12	10
β-strand	258-260	3	12
β-strand	267	1	13
β-strand	275	1	13
β-strand	280-287	8	12
β-strand	288-289	2	11
β-strand	296-300	5	11
β-strand	303	1	11
β-strand	307-314	8	11
α-helix	320-325	6
α-helix	332-335	4
β-strand	341-348	8	12
α-helix	349-351	3
β-strand	352-358	7	10
α-helix	359-362	4
α-helix	369-373	5
β-strand	392-401	10	10
β-strand	419-422	4	12
β-strand	427-433	7	11
β-strand	438-439	2	11
β-strand	442-445	4	11

Chains D, F and H: 16 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	33-34	2	21
α-helix	35-37	3
β-strand	38	1	22
α-helix	43-46	4
α-helix	48-60	13
α-helix	64-84	21
α-helix	85-87	3
β-strand	97	1	23
β-strand	100-101	2	24
α-helix	103-115	13
α-helix	121-129	9
α-helix	145-158	14
β-strand	170-179	10	23
α-helix	180-181	2
β-strand	186-187	2	21
α-helix	188-197	10
β-strand	201-203	3	23
β-strand	205	1	22
α-helix	211-226	16
β-strand	244-255	12	23
β-strand	258-260	3	25
β-strand	267	1	26
β-strand	274	1	27
β-strand	275	1	26
β-strand	280-287	8	25
β-strand	288-289	2	24
β-strand	296-300	5	24
β-strand	303	1	24
β-strand	307-314	8	24
α-helix	320-325	6
α-helix	332-335	4
β-strand	341-348	8	25
α-helix	349-351	3
β-strand	352-358	7	23
α-helix	359-362	4
α-helix	369-373	5
β-strand	392-401	10	23
β-strand	419-422	4	25
β-strand	427-433	7	24
β-strand	438-439	2	24
β-strand	442-445	4	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Renin	A, C, E, G	protein	383	HOMO SAPIENS	P00797 (AlphaFold model)
Angiotensinogen	B, D, F, H	protein	452	HOMO SAPIENS	P01019 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>2X0B_1 RENIN (chains A, C, E, G)
LPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMD
TQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGT
ELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAI
GRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIK
TGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVV
KCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGA
TFIRKFYTEFDRRNNRIGFALAR

Sequence of entity 2 (B, D, F, H), FASTA

>2X0B_2 ANGIOTENSINOGEN (chains B, D, F, H)
DRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVNEKALQDQLVLVAA
KLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDH
TADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFT
APGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVD
STLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQ
VPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQ
DLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLE
VTLNRPFLFAVYDQSATALHFLGRVANPLSTA

Primary citation

A Redox Switch in Angiotensinogen Modulates Angiotensin Release. Zhou, A., Carrell, R.W., Murphy, M.P. et al. Nature (2010) 468:108. DOI 10.1038/NATURE09505 · PubMed

Other PDB entries of the same protein (UniProt P00797 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3K1W 1.5 Å, New Classes of Potent and Bioavailable Human Renin Inhibitors
1HRN 1.8 Å, High resolution crystal structures of recombinant human renin in complex with…
2G24 1.9 Å, Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring
2IKO 1.9 Å, Crystal Structure of Human Renin Complexed with Inhibitor
3G72 1.9 Å, Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors
3KM4 1.9 Å, Optimization of Orally Bioavailable Alkyl Amine Renin Inhibitors
3G6Z 2.0 Å, Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors
3G70 2.0 Å, Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors
3GW5 2.0 Å, Crystal structure of human renin complexed with a novel inhibitor
3OWN 2.0 Å, Potent macrocyclic renin inhibitors
4Q1N 2.09 Å, Structure-based design of 4-hydroxy-3,5-substituted piperidines as direct renin inhibitors
2G26 2.1 Å, Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring

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