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3FYY

Crystal structure of divergent enolase from Oceanobacillus iheyensis complexed with Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP193
AGLU221
AHIS246
AHOH557
AHOH565

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH632
AASP42
AHIS45
ATHR297
AHOH631

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP193
BGLU221
BHIS246
BHOH411
BHOH630

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BASP42
BHIS45
BTHR297
BHOH633
BHOH634

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:19883118
ChainResidueDetails
ATYR90
BTYR90

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:19883118
ChainResidueDetails
ATYR164
BTYR164

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING:
ChainResidueDetails
AARG15
AARG385
BARG15
BASP42
BHIS45
BTYR89
BASP193
BGLU221
BHIS246
BTHR296
BTHR297
AASP42
BARG385
AHIS45
ATYR89
AASP193
AGLU221
AHIS246
ATHR296
ATHR297

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Increases basicity of active site Tyr
ChainResidueDetails
AARG162
BARG162

Catalytic Information from CSA
site_idMCSA1
Number of Residues9
DetailsM-CSA 502
ChainResidueDetails
AASP42metal ligand
AHIS45metal ligand
ATYR90proton acceptor, proton donor
AARG162electrostatic stabiliser, modifies pKa
ATYR164proton acceptor, proton donor
AASP193metal ligand
AGLU221metal ligand
AHIS246metal ligand
ATHR297metal ligand

site_idMCSA2
Number of Residues9
DetailsM-CSA 502
ChainResidueDetails
BASP42metal ligand
BHIS45metal ligand
BTYR90proton acceptor, proton donor
BARG162electrostatic stabiliser, modifies pKa
BTYR164proton acceptor, proton donor
BASP193metal ligand
BGLU221metal ligand
BHIS246metal ligand
BTHR297metal ligand

227344

PDB entries from 2024-11-13

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