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1LU0

Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0030414molecular_functionpeptidase inhibitor activity
B0004866molecular_functionendopeptidase inhibitor activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0030414molecular_functionpeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AGLU19
AGLU19
BGLU19
BGLU19

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 205
ChainResidue
BHOH347
AARG1
AARG1
AHOH357
BGLU19
BHOH347

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MRD B 204
ChainResidue
BARG5
BASP15
BCYS28
BGLY29
BGOL203
BHOH325

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
ACYS3
APRO4
AARG5
ASER14
AASP15
ACYS28
AHOH310
AHOH368

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 203
ChainResidue
AILE6
BGLU9
BMRD204
BHOH371

Functional Information from PROSITE/UniProt
site_idPS00286
Number of Residues20
DetailsSQUASH_INHIBITOR Squash family of serine protease inhibitors signature. CPrilleCkkDsDClaeCvC
ChainResidueDetails
ACYS3-CYS22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Reactive bond
ChainResidueDetails
AARG5
BARG5

238268

PDB entries from 2025-07-02

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