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6F4U

Crystal structure of reactive loop cleaved kallistatin at 1.9 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005615cellular_componentextracellular space
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 401
ChainResidue
ATYR64
AALA67
ASER68
AGLU290
AGLU291
AHOH530

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 402
ChainResidue
AASP57
AGLY106
AHOH623

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 403
ChainResidue
AGLY72
ALYS73
AASN74
DLYS426

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 404
ChainResidue
AGLU290
AGLU291
ALEU293
AHOH527

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 405
ChainResidue
AGLU69
AHOH522
AHOH652

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 406
ChainResidue
AASP258
AARG259
APHE310

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 407
ChainResidue
AGLU114
ASER115
AASP158
AVAL162
AGLU288
AHOH515

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 408
ChainResidue
AASP258
AARG259
ALEU261
APRO262
AASN282
AHOH554

site_idAC9
Number of Residues5
Detailsbinding site for residue CL A 409
ChainResidue
ALYS202
ASER360
ALYS361
AALA384
AHOH588

site_idAD1
Number of Residues5
Detailsbinding site for residue NA A 410
ChainResidue
ATYR270
AGLY272
AHOH541
AHOH605
AHOH619

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO D 501
ChainResidue
ATYR234
DASN400
DARG401

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. LRFNRPFLVvI
ChainResidueDetails
DLEU397-ILE407

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond
ChainResidueDetails
DPHE388

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN157

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490
ChainResidueDetails
AASN238

237735

PDB entries from 2025-06-18

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