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8P0I

Crystal structure of the open conformation of insulin-regulated aminopeptidase in complex with a small-MW inhibitor

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues11
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. SVVLDDGLvq.D
ChainResidueDetails
ASER336-ASP346

site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IIAHELAHQW
ChainResidueDetails
AILE461-TRP470

site_idPS01228
Number of Residues12
DetailsCOF_1 Hypothetical cof family signature 1. NLsqDVNGTLVS
ChainResidueDetails
AASN368-SER379

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU465
BGLU465

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU295
AGLY428
BGLU295
BGLY428

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AHIS464
AHIS468
AGLU487
BHIS464
BHIS468
BGLU487

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
ATYR549
BTYR549

site_idSWS_FT_FI5
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN184
AASN448
AASN682
AASN850
BASN184
BASN448
BASN682
BASN850

site_idSWS_FT_FI6
Number of Residues24
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN215
AASN760
AASN834
AASN989
BASN215
BASN256
BASN266
BASN368
BASN374
BASN525
BASN578
AASN256
BASN598
BASN664
BASN760
BASN834
BASN989
AASN266
AASN368
AASN374
AASN525
AASN578
AASN598
AASN664

227344

PDB entries from 2024-11-13

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