Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4MGG

Crystal structure of an enolase (mandelate racemase subgroup) from labrenzia aggregata iam 12614 (target nysgrc-012903) with bound mg, space group p212121

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0016597molecular_functionamino acid binding
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
A0071230biological_processcellular response to amino acid stimulus
A1901605biological_processalpha-amino acid metabolic process
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0016597molecular_functionamino acid binding
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0016853molecular_functionisomerase activity
B0046872molecular_functionmetal ion binding
B0071230biological_processcellular response to amino acid stimulus
B1901605biological_processalpha-amino acid metabolic process
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0016597molecular_functionamino acid binding
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
C0016853molecular_functionisomerase activity
C0046872molecular_functionmetal ion binding
C0071230biological_processcellular response to amino acid stimulus
C1901605biological_processalpha-amino acid metabolic process
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0016597molecular_functionamino acid binding
D0016829molecular_functionlyase activity
D0016836molecular_functionhydro-lyase activity
D0016853molecular_functionisomerase activity
D0046872molecular_functionmetal ion binding
D0071230biological_processcellular response to amino acid stimulus
D1901605biological_processalpha-amino acid metabolic process
E0000287molecular_functionmagnesium ion binding
E0003824molecular_functioncatalytic activity
E0016597molecular_functionamino acid binding
E0016829molecular_functionlyase activity
E0016836molecular_functionhydro-lyase activity
E0016853molecular_functionisomerase activity
E0046872molecular_functionmetal ion binding
E0071230biological_processcellular response to amino acid stimulus
E1901605biological_processalpha-amino acid metabolic process
F0000287molecular_functionmagnesium ion binding
F0003824molecular_functioncatalytic activity
F0016597molecular_functionamino acid binding
F0016829molecular_functionlyase activity
F0016836molecular_functionhydro-lyase activity
F0016853molecular_functionisomerase activity
F0046872molecular_functionmetal ion binding
F0071230biological_processcellular response to amino acid stimulus
F1901605biological_processalpha-amino acid metabolic process
G0000287molecular_functionmagnesium ion binding
G0003824molecular_functioncatalytic activity
G0016597molecular_functionamino acid binding
G0016829molecular_functionlyase activity
G0016836molecular_functionhydro-lyase activity
G0016853molecular_functionisomerase activity
G0046872molecular_functionmetal ion binding
G0071230biological_processcellular response to amino acid stimulus
G1901605biological_processalpha-amino acid metabolic process
H0000287molecular_functionmagnesium ion binding
H0003824molecular_functioncatalytic activity
H0016597molecular_functionamino acid binding
H0016829molecular_functionlyase activity
H0016836molecular_functionhydro-lyase activity
H0016853molecular_functionisomerase activity
H0046872molecular_functionmetal ion binding
H0071230biological_processcellular response to amino acid stimulus
H1901605biological_processalpha-amino acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
ALYS45

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI A 402
ChainResidue
AHIS98
AHOH501
AHOH502
GHIS98
GHOH501
GHOH502

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AHOH506
AHOH507
AHOH797
EHOH804
AGLY197
AHOH505

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 404
ChainResidue
AASP193
AGLU218
AASP241
AASN263
AHOH510
AHOH511
AHOH512

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP193
BGLU218
BASP241
BASN263
BHOH501
BHOH721
BHOH806

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BGLY197
BHOH503
BHOH504
BHOH505
BHOH506
DHOH503

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 403
ChainResidue
BALA143
BARG176

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI C 401
ChainResidue
CHIS98
CHOH501
CHOH502
EHIS98
EHOH802
EHOH803

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 402
ChainResidue
CGLY197
CHOH503
CHOH504
CHOH663
CHOH730
GHOH506

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG C 403
ChainResidue
CASP193
CGLU218
CASP241
CASN263
CLYS265
CHOH507
CHOH508
CHOH740

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI D 401
ChainResidue
DHIS98
DHOH501
HHIS98
HHOH501
HHOH502
HHOH503

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 402
ChainResidue
CHOH505
CHOH506
DGLY197
DHOH504
DHOH505
DHOH660

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG D 403
ChainResidue
DGLN163
DASP193
DGLU218
DASP241
DHOH512
DHOH525
DHOH540

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG E 401
ChainResidue
EASN24
EGLY197
EHOH805
EHOH806
EHOH807
EHOH1041
HHOH504

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG E 402
ChainResidue
EASP193
EGLU218
EASP241
EASN263
ELYS265
EHOH810
EHOH811
EHOH812

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG F 401
ChainResidue
AHOH504
FGLY197
FHOH501
FHOH502
FHOH503
FHOH703

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG F 402
ChainResidue
FHOH505
FHOH707
FASP193
FGLU218
FASP241
FHOH504

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG G 401
ChainResidue
GASP193
GGLU218
GASP241
GHOH507
GHOH508
GHOH509

site_idCC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG G 402
ChainResidue
GGLU157
GHOH510
GHOH511
GHOH512
GHOH513
GHOH514
GHOH664

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG G 403
ChainResidue
BHOH507
GGLY197
GHOH515
GHOH516
GHOH517
GHOH518

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG H 401
ChainResidue
HASP193
HGLU218
HASP241
HLYS265
HHOH505
HHOH506
HHOH507

site_idCC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG H 402
ChainResidue
FHOH506
HGLY197
HHOH508
HHOH509
HHOH510
HHOH641

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:25608448
ChainResidueDetails
ALYS165
ELYS265
FLYS165
FLYS265
GLYS165
GLYS265
HLYS165
HLYS265
ALYS265
BLYS165
BLYS265
CLYS165
CLYS265
DLYS165
DLYS265
ELYS165

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:25608448, ECO:0007744|PDB:4MGG
ChainResidueDetails
AASP193
DASP193
DGLU218
DASP241
EASP193
EGLU218
EASP241
FASP193
FGLU218
FASP241
GASP193
AGLU218
GGLU218
GASP241
HASP193
HGLU218
HASP241
AASP241
BASP193
BGLU218
BASP241
CASP193
CGLU218
CASP241

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon