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

3HPF

Crystal structure of the mutant Y90F of divergent galactarate dehydratase from Oceanobacillus iheyensis complexed with Mg and galactarate

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 Residues21
DetailsBINDING SITE FOR RESIDUE GAE A 411
ChainResidue
AARG15
APHE271
ATHR296
ATHR297
AGLN298
AARG385
AHOH397
AHOH398
AMG401
AMG402
AHOH518
AASP42
AHOH536
AHOH597
AHIS45
ATYR89
AARG162
ATYR164
AASP193
AGLU221
AHIS246

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP193
AGLU221
AHIS246
AHOH397
AGAE411

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AASP42
AHIS45
ATHR297
AGAE411

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GAE B 411
ChainResidue
BARG15
BASP42
BHIS45
BTYR89
BARG162
BTYR164
BASP193
BGLU221
BHIS246
BPHE271
BTHR296
BTHR297
BGLN298
BARG385
BMG401
BMG402
BHOH404
BHOH451
BHOH537
BHOH595
BHOH611

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP193
BGLU221
BHIS246
BHOH404
BGAE411

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BASP42
BHIS45
BTHR297
BGAE411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:19883118
ChainResidueDetails
APHE90
BPHE90

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
AASP193
AGLU221
AHIS246
ATHR296
ATHR297
AARG385
BARG15
BASP42
BHIS45
BTYR89
BASP193
BGLU221
BHIS246
BTHR296
BTHR297
BARG385
AARG15
AASP42
AHIS45
ATYR89

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
APHE90proton 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
BPHE90proton acceptor, proton donor
BARG162electrostatic stabiliser, modifies pKa
BTYR164proton acceptor, proton donor
BASP193metal ligand
BGLU221metal ligand
BHIS246metal ligand
BTHR297metal ligand

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon