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1SMP

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN SERRATIA MARCESCENS METALLO-PROTEASE AND AN INHIBITOR FROM ERWINIA CHRYSANTHEMI

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
I0004857molecular_functionenzyme inhibitor activity
I0004866molecular_functionendopeptidase inhibitor activity
I0008191molecular_functionmetalloendopeptidase inhibitor activity
I0010951biological_processnegative regulation of endopeptidase activity
I0030414molecular_functionpeptidase inhibitor activity
I0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 472
ChainResidue
AHIS176
AHIS180
AHIS186
ISER1

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 473
ChainResidue
AASP290
AARG253
AGLY255
ATHR257
AASP285
AGLY287

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 474
ChainResidue
AGLY288
AASP290
ATHR327
AGLU329
AHOH524
AHOH618

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 475
ChainResidue
AGLY334
AGLY336
AASP338
AGLY351
AALA353
AASP356

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 476
ChainResidue
AASN343
AALA345
AASN347
AGLY360
AGLY362
AASP365

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 477
ChainResidue
AGLY352
AGLY354
AASP356
AGLY369
AALA371
AASP374

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 478
ChainResidue
AGLY361
AGLY362
AGLY363
AASP365
AASP383
AASP390

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 479
ChainResidue
AGLY370
AGLY372
AASP374
AGLN396
AASP400
AHOH512

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU177
AGLU194

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU177

246704

PDB entries from 2025-12-24

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