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3JVA

Crystal structure of Dipeptide Epimerase from Enterococcus faecalis V583

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0006518biological_processpeptide metabolic process
A0009063biological_processamino acid catabolic process
A0016853molecular_functionisomerase activity
A0016854molecular_functionracemase and epimerase activity
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0006518biological_processpeptide metabolic process
B0009063biological_processamino acid catabolic process
B0016853molecular_functionisomerase activity
B0016854molecular_functionracemase and epimerase activity
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0006518biological_processpeptide metabolic process
C0009063biological_processamino acid catabolic process
C0016853molecular_functionisomerase activity
C0016854molecular_functionracemase and epimerase activity
C0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0006518biological_processpeptide metabolic process
D0009063biological_processamino acid catabolic process
D0016853molecular_functionisomerase activity
D0016854molecular_functionracemase and epimerase activity
D0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
D0046872molecular_functionmetal ion binding
E0000287molecular_functionmagnesium ion binding
E0006518biological_processpeptide metabolic process
E0009063biological_processamino acid catabolic process
E0016853molecular_functionisomerase activity
E0016854molecular_functionracemase and epimerase activity
E0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
E0046872molecular_functionmetal ion binding
F0000287molecular_functionmagnesium ion binding
F0006518biological_processpeptide metabolic process
F0009063biological_processamino acid catabolic process
F0016853molecular_functionisomerase activity
F0016854molecular_functionracemase and epimerase activity
F0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
F0046872molecular_functionmetal ion binding
G0000287molecular_functionmagnesium ion binding
G0006518biological_processpeptide metabolic process
G0009063biological_processamino acid catabolic process
G0016853molecular_functionisomerase activity
G0016854molecular_functionracemase and epimerase activity
G0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
G0046872molecular_functionmetal ion binding
H0000287molecular_functionmagnesium ion binding
H0006518biological_processpeptide metabolic process
H0009063biological_processamino acid catabolic process
H0016853molecular_functionisomerase activity
H0016854molecular_functionracemase and epimerase activity
H0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GOL A 355
ChainResidue
AGLU57
EGLU57
ETHR58
EGLY61
ETHR62
ATHR58
AGLY61
ATHR62
AHOH401
AHOH546
AHOH625
AHOH704
AHOH831

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 356
ChainResidue
AASP189
AGLU215
AASP240
ASO4357
AHOH358
AHOH359

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 A 357
ChainResidue
ALYS159
ALYS161
AASP189
AGLU215
AASP240
ALYS264
ACYS292
AASP318
AMG356
AHOH358
AHOH386
AHOH399

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 355
ChainResidue
BILE166
BTRP194
BASP198
BLYS201

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 356
ChainResidue
AMET1
AASN77
ALYS113
BLEU116
BPRO117
BGLN120
BGLU346

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 357
ChainResidue
BILE54
BLYS159
BLYS264
BCYS292
BHOH359
BHOH557
BHOH863

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 358
ChainResidue
BASP189
BGLU215
BASP240
BHOH359
BHOH360
BHOH362

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG C 355
ChainResidue
CASP189
CGLU215
CASP240
CSO4357
CHOH358
CHOH359
CHOH875

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 356
ChainResidue
CGLY56
CTHR58
CGLY61
GTHR58
GGLY61
GHOH836

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 C 357
ChainResidue
CLYS159
CLYS161
CLYS264
CCYS292
CMG355
CHOH358
CHOH762
CHOH875
CHOH877
CHOH879

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 355
ChainResidue
DASP189
DGLU215
DASP240
DHOH356
DHOH357
DHOH358

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 355
ChainResidue
EASP189
EGLU215
EASP240
ESO4356
EHOH357
EHOH358

site_idBC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 E 356
ChainResidue
EHOH357
EHOH399
EHOH400
ELYS159
ELYS161
EASP189
EGLU215
EASP240
ELYS264
ECYS292
EASP318
EMG355

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL F 355
ChainResidue
FILE54
FLYS159
FLYS264
FCYS292
FHOH360
FHOH428
FHOH775

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG F 356
ChainResidue
FASP189
FGLU215
FASP240
FHOH357
FHOH358
FHOH360

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG G 355
ChainResidue
GASP189
GGLU215
GASP240
GHOH357
GHOH358
GHOH359

site_idBC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 G 356
ChainResidue
GLYS159
GLYS161
GASP189
GLYS264
GCYS292
GHOH357
GHOH359
GHOH603

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG H 355
ChainResidue
HASP189
HGLU215
HASP240
HHOH356
HHOH359
HHOH360

Functional Information from PROSITE/UniProt
site_idPS00909
Number of Residues32
DetailsMR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LrlDaNqawtpkdAvkaiqaLadyqielVEQP
ChainResidueDetails
ALEU186-PRO217

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues112
DetailsBinding site: {}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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