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1AKL

ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080

Functional Information from GO Data
ChainGOidnamespacecontents
A0001869biological_processnegative regulation of complement activation, lectin pathway
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
A0010765biological_processpositive regulation of sodium ion transport
A0045959biological_processnegative regulation of complement activation, classical pathway
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
AHOH1061
AHIS176
AHIS180
AHIS186
ATYR216

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 501
ChainResidue
AARG253
AGLY255
ATHR257
AASP285
AGLY287
AASP290

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 502
ChainResidue
AGLY288
AASP290
ATHR327
AGLU329
AHOH1028
AHOH1252

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AGLY334
AGLY336
AASP338
AGLY351
AALA353
AASP356

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 504
ChainResidue
AGLY352
AALA353
AGLY354
AASP356
AGLY369
AGLY370
AALA371
AASP374

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 505
ChainResidue
AGLY370
AGLY372
AASP374
AGLN399
AASP400
AHOH1160

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 506
ChainResidue
AASN343
AVAL345
AASN347
AGLY360
ALEU362
AASP365

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 507
ChainResidue
AGLY361
AGLY363
AASP365
AGLU383
AASP390
AHOH1313

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 508
ChainResidue
AASP446
ASER448
AASP450
AHIS452
AASP454

site_idCAT
Number of Residues5
DetailsTHE ZINC ION AT THE BOTTOM OF CATALYTIC CLEFT HAS FIVE LIGANDS
ChainResidue
AHIS176
AHIS180
AHIS186
ATYR216
AHOH1061

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

site_idPS00330
Number of Residues19
DetailsHEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DiLygglGaDqLwGGagaD
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 Residues41
DetailsBINDING:
ChainResidueDetails
AARG253
AGLY255
ATHR257
AASP285
AGLY287
AGLY288
AASP290
ATHR327
AGLU329
AGLY334
AGLY336
AASP338
AASN343
AVAL345
AASN347
AGLY351
AGLY352
AALA353
AGLY354
AASP356
AGLY360
AGLY361
ALEU362
AGLY363
AASP365
AGLY369
AGLY370
AALA371
AGLY372
AASP374
AGLU383
AASP390
AASP400
AASP446
ASER448
AASP450
AHIS452
AASP454
AHIS176
AHIS180
AHIS186

221051

PDB entries from 2024-06-12

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