Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1W79

Crystal structure of the DD-transpeptidase-carboxypeptidase from Actinomadura R39

Functional Information from GO Data
ChainGOidnamespacecontents
A0000270biological_processpeptidoglycan metabolic process
A0004180molecular_functioncarboxypeptidase activity
A0004185molecular_functionserine-type carboxypeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008360biological_processregulation of cell shape
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016787molecular_functionhydrolase activity
A0046677biological_processresponse to antibiotic
A0071555biological_processcell wall organization
B0000270biological_processpeptidoglycan metabolic process
B0004180molecular_functioncarboxypeptidase activity
B0004185molecular_functionserine-type carboxypeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008360biological_processregulation of cell shape
B0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016787molecular_functionhydrolase activity
B0046677biological_processresponse to antibiotic
B0071555biological_processcell wall organization
C0000270biological_processpeptidoglycan metabolic process
C0004180molecular_functioncarboxypeptidase activity
C0004185molecular_functionserine-type carboxypeptidase activity
C0005576cellular_componentextracellular region
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008360biological_processregulation of cell shape
C0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016787molecular_functionhydrolase activity
C0046677biological_processresponse to antibiotic
C0071555biological_processcell wall organization
D0000270biological_processpeptidoglycan metabolic process
D0004180molecular_functioncarboxypeptidase activity
D0004185molecular_functionserine-type carboxypeptidase activity
D0005576cellular_componentextracellular region
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008360biological_processregulation of cell shape
D0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
D0009252biological_processpeptidoglycan biosynthetic process
D0016787molecular_functionhydrolase activity
D0046677biological_processresponse to antibiotic
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
ASER49
AHOH2431
AHOH2432
ASER298
ATHR393
ALYS410
ATHR411
AGLY412
ATHR413
AHOH2045
AHOH2430

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AHIS282
ATHR283
AHOH2282
AHOH2285
AHOH2286
AHOH2433

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AALA234
AARG236
AHOH2252
AHOH2434
AHOH2435
AHOH2436
AHOH2437
AHOH2438

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 510
ChainResidue
AGLU188
AHIS247
AGLU251

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 511
ChainResidue
AVAL406
AHIS462

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 B 500
ChainResidue
BSER49
BSER298
BLYS410
BTHR411
BGLY412
BTHR413
BHOH2418
BHOH2457
BHOH2458
BHOH2459
BHOH2460

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BASP281
BHIS282
BTHR283
BHOH2312
BHOH2316

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BARG236
BHOH2272
BHOH2461

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 C 500
ChainResidue
CSER49
CSER298
CTHR393
CLYS410
CTHR411
CGLY412
CTHR413
CHOH2045
CHOH2457
CHOH2458

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 501
ChainResidue
CASP281
CHIS282
CTHR283
CHOH2317
CHOH2459
CHOH2460

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 502
ChainResidue
CARG236
CHOH2461
CHOH2462
CHOH2463
CHOH2464

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 D 500
ChainResidue
DSER49
DSER298
DTHR393
DLYS410
DTHR411
DGLY412
DTHR413
DHOH2036
DHOH2410
DHOH2411
DHOH2412
DHOH2413

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 501
ChainResidue
DHIS282
DTHR283
DHOH2282
DHOH2283
DHOH2414
DHOH2415
DHOH2416

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 502
ChainResidue
DALA234
DARG236
DHOH2241
DHOH2417

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 510
ChainResidue
DMG511

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 511
ChainResidue
DMG510

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues692
DetailsRegion: {"description":"Absent in class-A beta-lactamases"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Acyl-ester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon