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4HX2

Crystal structure of Streptomyces caespitosus sermetstatin in complex with Bacillus licheniformis subtilisin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0046872molecular_functionmetal ion binding
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
C0008236molecular_functionserine-type peptidase activity
D0004867molecular_functionserine-type endopeptidase inhibitor activity
D0005576cellular_componentextracellular region
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
ATHR79
AVAL81

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AHOH420
AHOH423
AALA169
ATYR171
AVAL174

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 303
ChainResidue
AHIS238
AGLN275
AHOH476
CGLU112

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
ATYR209

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 1AX A 305
ChainResidue
AASN25
AGLY118
AMET119
AASP120
AARG145
AGLY146
AVAL147
APO4306
AHOH525

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 306
ChainResidue
AASP120
AGLY146
APRO239
ALEU241
A1AX305

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
AARG186
ATYR262
ATYR263
AHOH504

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA A 308
ChainResidue
AALA37
AHIS39
ALEU42
AASN43
AHOH449
AHOH543

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BHIS3
BCAC504
BHOH645
CASP120

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K B 502
ChainResidue
BHIS93
BASN104
BHOH652

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K B 503
ChainResidue
BHIS93
BHOH629

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CAC B 504
ChainResidue
BALA2
BHIS3
BASN85
BARG87
BZN501
BHOH645
CGLY118
CASP120

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 301
ChainResidue
CGLN2
CASP41
CLEU75
CASN77
CTHR79
CVAL81

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 302
ChainResidue
CALA169
CTYR171
CVAL174
CHOH401
CHOH447

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 303
ChainResidue
CLYS27
CTYR91
CASN117
CHOH414

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 304
ChainResidue
CARG186
CTYR262

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA C 305
ChainResidue
CASN62
CTYR209
DTYR72

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA D 201
ChainResidue
DHIS93
DTHR94
DASN104

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH
ChainResidueDetails
AVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA
ChainResidueDetails
AHIS64-ALA74

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG
ChainResidueDetails
AGLY219-GLY229

222415

PDB entries from 2024-07-10

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