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1OM7

CRYSTAL STRUCTURE OF A COLD ADAPTED ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18, SOAKED IN 85 mM EDTA

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 701
ChainResidue
AARG250
AASP252
ATHR254
AASP282
AGLY284
AASP287

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 703
ChainResidue
AGLY348
AALA350
AASP353
AGLY331
AGLY333
AASP335

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 704
ChainResidue
AALA350
AGLY351
AASP353
AGLY366
ATHR368
AASP371

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 705
ChainResidue
AASN340
AALA342
AASN344
AGLY357
AGLY359
AASP362

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 706
ChainResidue
AGLY358
AGLY359
AGLY360
AASP362
AASP380
AASP387

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
AARG139
ATRP210
ASER211
AASN214
AHOH1368

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLTHEIGHTL
ChainResidueDetails
ATHR166-LEU175

site_idPS00330
Number of Residues19
DetailsHEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DiIygggGaDvLwGGtgsD
ChainResidueDetails
AASP353-ASP371

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qib
ChainResidueDetails
AGLU170

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PDB entries from 2024-11-06

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