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3T41

1.95 Angstrom Resolution Crystal Structure of Epidermin Leader Peptide Processing Serine Protease (EpiP) S393A Mutant from Staphylococcus aureus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 458
ChainResidue
AVAL323
ATHR325
AASP347
AHOH474
AHOH502
AHOH510
AHOH536

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 459
ChainResidue
AHOH616
AHOH637
AHOH686
ASER319
AHOH543

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 460
ChainResidue
ALYS280
AHOH561
AHOH567
AHOH655
AHOH656
AHOH693

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 458
ChainResidue
BVAL323
BTHR325
BASP347
BHOH464
BHOH482
BHOH498
BHOH511

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 459
ChainResidue
BSER319
BHOH556
BHOH558
BHOH623
BHOH665
BHOH676
BHOH691

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 460
ChainResidue
BLYS280
BHOH579
BHOH605
BHOH626
BHOH647
BHOH677
BHOH678

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 461
ChainResidue
BARG111
BASN116
BHOH628

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. IAIIDTGVmknH
ChainResidueDetails
AILE136-HIS147

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PDB entries from 2024-10-02

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