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Structure for peptidase A01.007: renin

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

 

PDB Organism Resolution Comment
2REN Homo sapiens 2.50 Å recombinant
Active site residues are shown in ball-and-stick representation: Asp104 and Asp292 in pink, and Tyr149 in green. N-Acetyl-D-glucosamine is shown in yellow in CPK representation. Some loops are not shown because of poor electron density.
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TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
Homo sapiens
recombinant glycosylated form 2.80 Å 1BBS 1BBS 1BBS 1BBS 1BBS 1BBS Dhanaraj et al., 1992
complex with butanediamide inhibitor BILA 1908 2.40 Å 1BIL 1BIL 1BIL 1BIL 1BIL 1BIL Tong et al., 1995
complex with butanediamide inhibitor BILA 2151 2.80 Å 1BIM 1BIM 1BIM 1BIM 1BIM 1BIM Tong et al., 1995
complex with polyhydroxymonoamide inhibitor BILA 980 1.80 Å 1HRN 1HRN 1HRN 1HRN 1HRN 1HRN Tong et al., 1995
complex with CGP 38,560 2.40 Å 1RNE 1RNE 1RNE 1RNE 1RNE 1RNE Rahuel et al., 1991
complex with PF00074777 2.20 Å 2BKS 2BKS 2BKS 2BKS 2BKS 2BKS Powell et al., 2005
complex with PF00257567 2.30 Å 2BKT 2BKT 2BKT 2BKT 2BKT 2BKT Powell et al., 2005
ketopiperazine-based renin inhibitors: optimization of the c ring 2.20 Å 2FS4 2FS4 2FS4 2FS4 2FS4 2FS4 Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the "c" ring 2.90 Å 2G1N 2G1N 2G1N 2G1N 2G1N 2G1N Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the "c" ring 2.70 Å 2G1O 2G1O 2G1O 2G1O 2G1O 2G1O Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the c ring 2.42 Å 2G1R 2G1R 2G1R 2G1R 2G1R 2G1R Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the c ring 2.50 Å 2G1S 2G1S 2G1S 2G1S 2G1S 2G1S Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the "c" ring 2.50 Å 2G1Y 2G1Y 2G1Y 2G1Y 2G1Y 2G1Y Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the c ring 2.40 Å 2G20 2G20 2G20 2G20 2G20 2G20 Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the "c" ring 2.20 Å 2G21 2G21 2G21 2G21 2G21 2G21 Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the "c" ring 2.50 Å 2G22 2G22 2G22 2G22 2G22 2G22 Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the "c" ring 1.90 Å 2G24 2G24 2G24 2G24 2G24 2G24 Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the "c" ring 2.10 Å 2G26 2G26 2G26 2G26 2G26 2G26 Holsworth et al., 2006
ketopiperazine-based renin inhibitors: optimization of the "c" ring 2.90 Å 2G27 2G27 2G27 2G27 2G27 2G27 Holsworth et al., 2006
complex with PF02342674 2.30 Å 2I4Q 2I4Q 2I4Q 2I4Q 2I4Q 2I4Q Powell et al., 2007
complex with 5-4-[(3,5-difluorobenzyl)amino]phenyl-6-ethylpyrimidine-2,4-diamine 1.90 Å 2IKO 2IKO 2IKO 2IKO 2IKO 2IKO Sarver et al., 2007
complex with 6-ethyl-5-[(2S)-1-(3-methoxypropyl)-2-phenyl-1,2,3,4-tetrahydroquinolin-7-yl]pyrimidine-2,4-diamine 2.60 Å 2IKU 2IKU 2IKU 2IKU 2IKU 2IKU Sarver et al., 2007
complex with N-[2-(2-amino-6-ethyl-5-[4-(3-methoxypropyl)-2,2-dimethyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-6-yl]pyrimidin-4-ylamino)ethyl]naphthalene-2-sulfonamide 2.24 Å 2IL2 2IL2 2IL2 2IL2 2IL2 2IL2 Sarver et al., 2007
recombinant 2.50 Å 2REN 2REN 2REN 2REN 2REN 2REN Sielecki et al., 1989
complex with inhibitor 10 (aliskiren) 2.20 Å 2V0Z 2V0Z 2V0Z 2V0Z 2V0Z 2V0Z Rahuel et al., 2000
complex with inhibitor 9 ((2R,4S,5S,7S)-5-amino-N-butyl-4-hydroxy-7-[4-methoxy-3-(3-methoxypropoxy)benzyl]-2,8-dimethylnonanamide) 3.10 Å 2V10 2V10 2V10 2V10 2V10 2V10 Rahuel et al., 2000
complex with inhibitor 6 ((2S,4S,5R,7R)-4-amino-8-(butylamino)-5-hydroxy-2,7-dimethyl-8-oxooctyl 1-benzyl-1H-indole-3-carboxylate) 3.10 Å 2V11 2V11 2V11 2V11 2V11 2V11 Rahuel et al., 2000
complex with inhibitor 8 (N-[(2S,4S,5S,7R)-4-amino-8-(butylamino)-5-hydroxy-7-methyl-2-(1-methylethyl)-8-oxooctyl]-2-(3-methoxypropoxy)benzamide) 3.20 Å 2V12 2V12 2V12 2V12 2V12 2V12 Rahuel et al., 2000
complex with inhibitor 7 (N-[(2R,4S,5S,7R)-4-amino-8-(butylamino)-5-hydroxy-2,7-dimethyl-8-oxooctyl]-2-(3-methoxypropoxy)benzamide) 2.80 Å 2V13 2V13 2V13 2V13 2V13 2V13 Rahuel et al., 2000
complex with inhibitor 3 2.80 Å 2V16 2V16 2V16 2V16 2V16 2V16 Rahuel et al., 1991
complex with inhibitor 3 2.80 Å 2V16 2V16 2V16 2V16 2V16 2V16 Rahuel et al., 1991
complex with human angiotensinogen 4.33 Å 2X0B 2X0B 2X0B 2X0B 2X0B 2X0B Zhou et al., 2010
complex with remikiren 2.20 Å 3D91 3D91 3D91 3D91 3D91 3D91 Mathews et al., 1996
mature  peptidase 2.00 Å 3G6Z 3G6Z 3G6Z 3G6Z 3G6Z 3G6Z Bezencon et al., 2009
mature  peptidase 2.00 Å 3G70 3G70 3G70 3G70 3G70 3G70 Bezencon et al., 2009
mature  peptidase 1.90 Å 3G72 3G72 3G72 3G72 3G72 3G72 Bezencon et al., 2009
mature  peptidase 2.00 Å 3GW5 3GW5 3GW5 3GW5 3GW5 3GW5 Tice et al., 2009
mature  peptidase 1.50 Å 3K1W 3K1W 3K1W 3K1W 3K1W 3K1W Remen et al., 2009
mature  peptidase 1.90 Å 3KM4 3KM4 3KM4 3KM4 3KM4 3KM4 Xu et al., 2010
mature  peptidase 2.40 Å 3O9L 3O9L 3O9L 3O9L 3O9L 3O9L Corminboeuf et al., 2010
mature  peptidase 2.17 Å 3OAD 3OAD 3OAD 3OAD 3OAD 3OAD Corminboeuf et al., 2010
complex with piperidine inhibitor 2.30 Å 3OAG 3OAG 3OAG 3OAG 3OAG 3OAG Corminboeuf et al., 2010
mature  peptidase 2.55 Å 3OOT 3OOT 3OOT 3OOT 3OOT 3OOT Scheiper et al., 2010
mature  peptidase 2.78 Å 3OQF 3OQF 3OQF 3OQF 3OQF 3OQF Scheiper et al., 2010
mature  peptidase 2.90 Å 3OQK 3OQK 3OQK 3OQK 3OQK 3OQK Scheiper et al., 2010
mature  peptidase 2.00 Å 3OWN 3OWN 3OWN 3OWN 3OWN 3OWN Sund et al., 2011
mature  peptidase 2.60 Å 3Q3T 3Q3T 3Q3T 3Q3T 3Q3T 3Q3T Yuan et al., 2011
mature  peptidase 2.19 Å 3Q4B 3Q4B 3Q4B 3Q4B 3Q4B 3Q4B Jia et al., 2011
mature  peptidase 2.16 Å 3Q5H 3Q5H 3Q5H 3Q5H 3Q5H 3Q5H Jia et al., 2011
mature  peptidase 2.10 Å 3SFC 3SFC 3SFC 3SFC 3SFC 3SFC Scheiper et al., 2011
mature  peptidase 2.93 Å 3VCM 3VCM 3VCM 3VCM 3VCM 3VCM Morales et al., 2012
mature  peptidase 3.00 Å 3VSW 3VSW 3VSW 3VSW 3VSW 3VSW Nakamura et al., 2012
mature  peptidase 2.80 Å 3VSX 3VSX 3VSX 3VSX 3VSX 3VSX Nakamura et al., 2012
mature  peptidase 2.60 Å 3VUC 3VUC 3VUC 3VUC 3VUC 3VUC
mature  peptidase 2.81 Å 3VYD 3VYD 3VYD 3VYD 3VYD 3VYD Mori et al., 2012
mature  peptidase 2.70 Å 3VYE 3VYE 3VYE 3VYE 3VYE 3VYE Mori et al., 2012
mature  peptidase 2.80 Å 3VYF 3VYF 3VYF 3VYF 3VYF 3VYF Mori et al., 2012
mature  peptidase 2.60 Å 4AMT 4AMT 4AMT 4AMT 4AMT 4AMT
mature  peptidase 2.40 Å 4GJ5 4GJ5 4GJ5 4GJ5 4GJ5 4GJ5 Lorthiois et al., 2013
mature  peptidase 2.58 Å 4GJ6 4GJ6 4GJ6 4GJ6 4GJ6 4GJ6 Lorthiois et al., 2013
mature  peptidase 2.80 Å 4GJ7 4GJ7 4GJ7 4GJ7 4GJ7 4GJ7 Lorthiois et al., 2013
mature  peptidase 2.50 Å 4GJ8 4GJ8 4GJ8 4GJ8 4GJ8 4GJ8 Ostermann et al., 2013
mature  peptidase 2.60 Å 4GJ9 4GJ9 4GJ9 4GJ9 4GJ9 4GJ9 Ostermann et al., 2013
mature  peptidase 2.60 Å 4GJA 4GJA 4GJA 4GJA 4GJA 4GJA Ostermann et al., 2013
mature  peptidase 2.75 Å 4GJB 4GJB 4GJB 4GJB 4GJB 4GJB Ostermann et al., 2013
mature  peptidase 2.40 Å 4GJC 4GJC 4GJC 4GJC 4GJC 4GJC Ostermann et al., 2013
mature  peptidase 2.65 Å 4GJD 4GJD 4GJD 4GJD 4GJD 4GJD Ostermann et al., 2013
mature  peptidase 2.65 Å 4PYV 4PYV 4PYV 4PYV 4PYV 4PYV Ehara et al., 2014
mature  peptidase 2.09 Å 4Q1N 4Q1N 4Q1N 4Q1N 4Q1N 4Q1N Ehara et al., 2014
mature  peptidase 2.45 Å 4RYC 4RYC 4RYC 4RYC 4RYC 4RYC Lorthiois et al., 2015
mature  peptidase 2.65 Å 4RYG 4RYG 4RYG 4RYG 4RYG 4RYG Lorthiois et al., 2015
mature  peptidase 2.60 Å 4RZ1 4RZ1 4RZ1 4RZ1 4RZ1 4RZ1 Sellner et al., 2015
mature  peptidase 2.10 Å 4S1G 4S1G 4S1G 4S1G 4S1G 4S1G McKittrick et al., 2015
mature  peptidase 2.40 Å 4XX3 4XX3 4XX3 4XX3 4XX3 4XX3
mature  peptidase 2.40 Å 4XX4 4XX4 4XX4 4XX4 4XX4 4XX4
discovery of tak-272: a novel, potent and orally active renin in- hibitor ***caveat 5koq nag b 401 has wrong chirality at atom c1 2.70 Å 5KOQ 5KOQ 5KOQ 5KOQ 5KOQ 5KOQ
discovery of tak-272: a novel, potent and orally active renin in- hibitor 2.41 Å 5KOS 5KOS 5KOS 5KOS 5KOS 5KOS
discovery of tak-272: a novel, potent and orally active renin in- hibitor 2.10 Å 5KOT 5KOT 5KOT 5KOT 5KOT 5KOT
structure-based design of a new series of n-piperidin-3-ylpyrimidine- 5-carboxamides as renin inhibitors 2.10 Å 5SXN 5SXN 5SXN 5SXN 5SXN 5SXN
structure-based design of a new series of n-piperidin-3-ylpyrimidine- 5-carboxamides as renin inhibitors 2.25 Å 5SY2 5SY2 5SY2 5SY2 5SY2 5SY2
structure-based design of a new series of n-piperidin-3-ylpyrimidine- 5-carboxamides as renin inhibitors 2.30 Å 5SY3 5SY3 5SY3 5SY3 5SY3 5SY3
structure-based design of a new series of n-piperidin-3-ylpyrimidine- 5-carboxamides as renin inhibitors 2.85 Å 5SZ9 5SZ9 5SZ9 5SZ9 5SZ9 5SZ9
novel approach of fragment-based lead discovery applied to renin inhibitors 2.64 Å 5T4S 5T4S 5T4S 5T4S 5T4S 5T4S
optimization of 3,5-disubstitued piperidine: discovery of non-peptide mimetics as an orally active renin inhibitor 2.20 Å 5TMG 5TMG 5TMG 5TMG 5TMG 5TMG
optimization of 3,5-disubstitued piperidine: discovery of non-peptide mimetics as an orally active renin inhibitor 2.65 Å 5TMK 5TMK 5TMK 5TMK 5TMK 5TMK
complex with a biphenylpipderidinylcarbinol 2.60 Å 5V8V 5V8V 5V8V 5V8V 5V8V 5V8V
complex with a biphenylpipderidinylcarbinol 2.90 Å 5VPM 5VPM 5VPM 5VPM 5VPM 5VPM
complex with a biphenylpipderidinylcarbinol 3.22 Å 5VRP 5VRP 5VRP 5VRP 5VRP 5VRP
complex with human angiotensinogen 2.55 Å 6I3F 6I3F 6I3F 6I3F 6I3F 6I3F

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