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4EAC

Crystal structure of mannonate dehydratase from Escherichia coli strain K12

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0006064biological_processglucuronate catabolic process
A0006974biological_processDNA damage response
A0008198molecular_functionferrous iron binding
A0008927molecular_functionmannonate dehydratase activity
A0016829molecular_functionlyase activity
A0030145molecular_functionmanganese ion binding
A0042840biological_processD-glucuronate catabolic process
B0005975biological_processcarbohydrate metabolic process
B0006064biological_processglucuronate catabolic process
B0006974biological_processDNA damage response
B0008198molecular_functionferrous iron binding
B0008927molecular_functionmannonate dehydratase activity
B0016829molecular_functionlyase activity
B0030145molecular_functionmanganese ion binding
B0042840biological_processD-glucuronate catabolic process
C0005975biological_processcarbohydrate metabolic process
C0006064biological_processglucuronate catabolic process
C0006974biological_processDNA damage response
C0008198molecular_functionferrous iron binding
C0008927molecular_functionmannonate dehydratase activity
C0016829molecular_functionlyase activity
C0030145molecular_functionmanganese ion binding
C0042840biological_processD-glucuronate catabolic process
D0005975biological_processcarbohydrate metabolic process
D0006064biological_processglucuronate catabolic process
D0006974biological_processDNA damage response
D0008198molecular_functionferrous iron binding
D0008927molecular_functionmannonate dehydratase activity
D0016829molecular_functionlyase activity
D0030145molecular_functionmanganese ion binding
D0042840biological_processD-glucuronate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
AARG6
AARG349
APRO350
AASP351
AARG373

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AHOH764
AHIS233
ACYS271
AHIS298
AASP351

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 401
ChainResidue
BARG6
BARG349
BPRO350
BASP351
BARG373

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 402
ChainResidue
BHIS233
BCYS271
BHIS298
BASP351
BHOH739

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 401
ChainResidue
CARG6
CARG349
CASP351
CARG373

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 402
ChainResidue
CHIS233
CCYS271
CHIS298
CASP351
CHOH692

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL D 401
ChainResidue
DARG6
DARG349
DASP351
DARG373

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN D 402
ChainResidue
DHIS233
DCYS271
DHIS298
DASP351
DHOH642

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 963
ChainResidueDetails
AHIS233metal ligand
ACYS271metal ligand
AHIS298metal ligand
AASP351metal ligand
AHIS352proton acceptor, proton donor
ATYR368proton acceptor, proton donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 963
ChainResidueDetails
BHIS233metal ligand
BCYS271metal ligand
BHIS298metal ligand
BASP351metal ligand
BHIS352proton acceptor, proton donor
BTYR368proton acceptor, proton donor

site_idMCSA3
Number of Residues6
DetailsM-CSA 963
ChainResidueDetails
CHIS233metal ligand
CCYS271metal ligand
CHIS298metal ligand
CASP351metal ligand
CHIS352proton acceptor, proton donor
CTYR368proton acceptor, proton donor

site_idMCSA4
Number of Residues6
DetailsM-CSA 963
ChainResidueDetails
DHIS233metal ligand
DCYS271metal ligand
DHIS298metal ligand
DASP351metal ligand
DHIS352proton acceptor, proton donor
DTYR368proton acceptor, proton donor

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PDB entries from 2025-12-17

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