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

4MUR

Crystal structure of vancomycin resistance D,D-dipeptidase/D,D-pentapeptidase VanXYc D59S mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004180molecular_functioncarboxypeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004180molecular_functioncarboxypeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AHIS95
AASP102
AHIS156
AHOH383
AHOH465

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 202
ChainResidue
AGLN67
AALA88
ASER93
AHOH598

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
AARG69
AHOH528
BLEU22

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 204
ChainResidue
AASN8
AASN10
AHIS11
AHOH470

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PE3 A 205
ChainResidue
AHIS179

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PE3 A 206
ChainResidue
AMET1
AASN2
AGLN5
ALYS14
AGLN17

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PE3 A 207
ChainResidue
AGLU37
ALYS40
AGLN41
AARG44

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PE3 A 208
ChainResidue
APHE189
BHIS179
BALA183
BHOH574

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 201
ChainResidue
BHIS95
BASP102
BHIS156
BHOH353
BHOH385

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 202
ChainResidue
AARG119
BLYS65
BARG68
BARG69
BHOH411
BHOH480
BHOH563

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 203
ChainResidue
BGLN67
BALA88
BHOH583

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 204
ChainResidue
AHIS21
ALEU22
AHOH580
BARG69

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 205
ChainResidue
AHOH538
BTHR63
BHOH436

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: catalytic acid/base residue => ECO:0000269|PubMed:24711382
ChainResidueDetails
AGLU153
BGLU153

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:4OAK
ChainResidueDetails
AGLU66
BGLU66

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:24711382, ECO:0007744|PDB:4OAK
ChainResidueDetails
AGLN67
AALA88
ASER93
ATRP155
BGLN67
BALA88
BSER93
BTRP155

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:4MUR, ECO:0007744|PDB:4MUS
ChainResidueDetails
AHIS95
AASP102
AHIS156
BHIS95
BASP102
BHIS156

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon