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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
A0016787molecular_functionhydrolase activity
A0031012cellular_componentextracellular matrix
A0045959biological_processnegative regulation of complement activation, classical pathway
A0046872molecular_functionmetal ion binding
A0141141biological_processsymbiont-mediated evasion of recognition by host pattern recognition receptor
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 Residues13
DetailsRepeat: {"description":"Hemolysin-type calcium-binding 1","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsRepeat: {"description":"Hemolysin-type calcium-binding 2","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues17
DetailsRepeat: {"description":"Hemolysin-type calcium-binding 3","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues41
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

247536

PDB entries from 2026-01-14

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