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1AF0

SERRATIA PROTEASE IN COMPLEX WITH INHIBITOR

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
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 472
ChainResidue
AHIS176
AHIS180
AHIS186
A0Z9674

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 474
ChainResidue
AASP290
AARG253
AGLY255
ATHR257
AASP285
AGLY287

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 476
ChainResidue
AGLY288
AASP290
ATHR327
AGLU329
AHOH2057
AHOH2059

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 478
ChainResidue
AGLY334
AGLY336
AASP338
AGLY351
AALA353
AASP356

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 480
ChainResidue
AASN343
AALA345
AASN347
AGLY360
AGLY362
AASP365

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 482
ChainResidue
AGLY352
AGLY354
AASP356
AGLY369
AALA371
AASP374

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 484
ChainResidue
AGLY370
AGLY372
AASP374
AASP400
AHOH2081
AHOH2141

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 486
ChainResidue
AGLY361
AGLY362
AGLY363
AASP365
AASP383
AASP390
AHOH2076

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0Z9 A 674
ChainResidue
AALA134
ATYR135
AALA136
ALEU138
AHIS176
AGLU177
AHIS180
AHIS186
AASN191
AALA192
ATYR216
AZN472

site_idACT
Number of Residues4
DetailsACTIVE SITE, HISTIDINES ARE ZINC LIGANDS AND E 177 THE PUTATIVE CATALYTIC BASE. TYR 216 IS INVOLVED IN LIGAND BINDING.
ChainResidue
AHIS176
AGLU177
AHIS180
AHIS186

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 Residues1
DetailsACT_SITE:
ChainResidueDetails
AGLU177

site_idSWS_FT_FI2
Number of Residues37
DetailsBINDING:
ChainResidueDetails
AHIS176
AGLY288
AASP290
ATHR327
AGLU329
AGLY334
AGLY336
AASP338
AASN343
AALA345
AASN347
AHIS180
AGLY351
AGLY352
AALA353
AGLY354
AASP356
AGLY360
AGLY361
AGLY362
AGLY363
AASP365
AHIS186
AGLY369
AGLY370
AALA371
AGLY372
AASP374
AASP383
AASP390
AASP400
ATYR216
AARG253
AGLY255
ATHR257
AASP285
AGLY287

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

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PDB entries from 2024-07-17

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