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4I35

The crystal structure of serralysin

Functional Information from GO Data
ChainGOidnamespacecontents
A0001907biological_processsymbiont-mediated killing of host cell
A0004222molecular_functionmetalloendopeptidase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0031012cellular_componentextracellular matrix
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AASP168
AHOH1040
AHIS229
ATYR230
AALA231
AALA232
ALYS278
AILE280
AHOH913
AHOH971

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
ATHR4
AASP7
ATYR130
AASN157
ASER405
ALYS409
AHOH874
AHOH924

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
ATRP46
AASN47
AVAL56
ALYS57
AASN114

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
AHIS16
AARG18
ALYS308
ASER309
AHOH656
AHOH947
AHOH999
AHOH1096
AHOH1097
AHOH1163

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
AASN101
AALA248
AASN249
ALEU250
ASER251
AASN275
AHOH715
AHOH910

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HEX A 506
ChainResidue
APRO197
ATYR216
ATRP217

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HEX A 507
ChainResidue
ATYR135
AALA136
APHE137
AOCT508

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OCT A 508
ChainResidue
APHE137
ATRP143
AHEX507

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OCT A 509
ChainResidue
AGLN34
ALEU37
APHE38

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 510
ChainResidue
AHIS176
AHIS180
AHIS186
ATYR216
AHOH1024

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 511
ChainResidue
AARG253
AGLY255
ATHR257
AASP285
AGLY287
AASP290

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 512
ChainResidue
AGLY288
AASP290
ATHR327
AGLU329
AHOH1051
AHOH1053

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 513
ChainResidue
AGLY334
AGLY336
AASP338
AGLY351
AALA353
AASP356

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 514
ChainResidue
AASN343
AALA345
AASN347
AGLY360
AGLY362
AASP365

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 515
ChainResidue
AGLY352
AGLY354
AASP356
AGLY369
AALA371
AASP374

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 516
ChainResidue
AGLY370
AGLY372
AASP374
AASP400
AHOH1076
AHOH1134

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 517
ChainResidue
AASP383
AASP390
AHOH1071
AGLY361
AGLY362
AGLY363
AASP365

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TFTHEIGHAL
ChainResidueDetails
ATHR173-LEU182

site_idPS00330
Number of Residues19
DetailsHEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DvLfgggGaDeLwGGagkD
ChainResidueDetails
AASP356-ASP374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsRepeat: {"description":"Hemolysin-type calcium-binding 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues17
DetailsRepeat: {"description":"Hemolysin-type calcium-binding 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues37
DetailsBinding site: {}
ChainResidueDetails

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PDB entries from 2025-12-24

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