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2GSH

Crystal structure of L-rhamnonate dehydratase from Salmonella typhimurium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0046872molecular_functionmetal ion binding
A0050032molecular_functionL-rhamnonate dehydratase activity
B0000287molecular_functionmagnesium ion binding
B0009063biological_processamino acid catabolic process
B0016052biological_processcarbohydrate catabolic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0046872molecular_functionmetal ion binding
B0050032molecular_functionL-rhamnonate dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 414
ChainResidue
BASP226
BGLU252
BGLU280
BHOH419
BHOH481

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 414
ChainResidue
AHOH480
AASP226
AGLU252
AGLU280
AHOH418

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 415
ChainResidue
AASP232
AVAL233
AASN234
BASP297
BGLY323
BLEU325

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 416
ChainResidue
AASP297
AGLN324
ALEU325
BASP232
BVAL233
BASN234

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. TiSCVDlALwDLfGKvvglPVykLLG
ChainResidueDetails
ATHR136-GLY161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS329
BHIS329

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AHIS33
BGLU252
BGLU280
BGLU349
AARG59
AASP226
AGLU252
AGLU280
AGLU349
BHIS33
BARG59
BASP226

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Increases basicity of active site His
ChainResidueDetails
AASP302
BASP302

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AGLU349
BGLU349

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 962
ChainResidueDetails
AASP226metal ligand
AGLU252metal ligand
AGLU280metal ligand
AASP302increase acidity, increase basicity, modifies pKa
AHIS329proton acceptor, proton donor, proton relay
AGLU349electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 962
ChainResidueDetails
BASP226metal ligand
BGLU252metal ligand
BGLU280metal ligand
BASP302increase acidity, increase basicity, modifies pKa
BHIS329proton acceptor, proton donor, proton relay
BGLU349electrostatic stabiliser

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PDB entries from 2024-04-24

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