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5H7V

Structure of full-length extracellular domain of HAI-1 at pH 4.6

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGClgnknnYlreeeC
ChainResidueDetails
APHE278-CYS296
APHE403-CYS421

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIdsfle.CDdtpNCpda.SDEaa...C
ChainResidueDetails
ACYS331-CYS353

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues83
DetailsDomain: {"description":"MANSC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00341","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues50
DetailsDomain: {"description":"BPTI/Kunitz inhibitor 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues50
DetailsDomain: {"description":"BPTI/Kunitz inhibitor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Reactive bond","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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