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1MPY

STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008198molecular_functionferrous iron binding
A0009056biological_processcatabolic process
A0018577molecular_functioncatechol 2,3-dioxygenase activity
A0042203biological_processtoluene catabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0003824molecular_functioncatalytic activity
B0008198molecular_functionferrous iron binding
B0009056biological_processcatabolic process
B0018577molecular_functioncatechol 2,3-dioxygenase activity
B0042203biological_processtoluene catabolic process
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
C0003824molecular_functioncatalytic activity
C0008198molecular_functionferrous iron binding
C0009056biological_processcatabolic process
C0018577molecular_functioncatechol 2,3-dioxygenase activity
C0042203biological_processtoluene catabolic process
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
D0003824molecular_functioncatalytic activity
D0008198molecular_functionferrous iron binding
D0009056biological_processcatabolic process
D0018577molecular_functioncatechol 2,3-dioxygenase activity
D0042203biological_processtoluene catabolic process
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 308
ChainResidue
AHIS153
AHIS214
ASER216
AGLU265
AACN309

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 B 308
ChainResidue
BGLU265
BACN309
BHIS153
BHIS214
BSER216
BTYR255

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 C 308
ChainResidue
CHIS153
CHIS214
CSER216
CGLU265
CACN309

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 D 308
ChainResidue
DHIS153
DHIS214
DSER216
DGLU265
DACN309

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACN A 309
ChainResidue
APHE191
AHIS246
ALEU248
ATHR249
ATYR255
AFE2308

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACN B 309
ChainResidue
BHIS246
BLEU248
BTHR249
BTYR255
BFE2308

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACN C 309
ChainResidue
CHIS246
CLEU248
CTYR255
CFE2308

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACN D 309
ChainResidue
DLEU155
DHIS246
DTYR255
DILE291
DFE2308

Functional Information from PROSITE/UniProt
site_idPS00082
Number of Residues22
DetailsEXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. TrHglthgktIYffDPsGnrnE
ChainResidueDetails
ATHR244-GLU265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AHIS153
DHIS153
DHIS214
DGLU265
AHIS214
AGLU265
BHIS153
BHIS214
BGLU265
CHIS153
CHIS214
CGLU265

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10368270
ChainResidueDetails
AHIS199
AHIS246
ATYR255

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10368270
ChainResidueDetails
BHIS199
BHIS246
BTYR255

site_idCSA3
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10368270
ChainResidueDetails
CHIS199
CHIS246
CTYR255

site_idCSA4
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10368270
ChainResidueDetails
DHIS199
DHIS246
DTYR255

site_idMCSA1
Number of Residues6
DetailsM-CSA 34
ChainResidueDetails
AHIS153metal ligand
AHIS199hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS214metal ligand
AHIS246polar/non-polar interaction, steric role
ATYR255polar/non-polar interaction, steric role
AGLU265metal ligand

site_idMCSA2
Number of Residues6
DetailsM-CSA 34
ChainResidueDetails
BHIS153metal ligand
BHIS199hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS214metal ligand
BHIS246polar/non-polar interaction, steric role
BTYR255polar/non-polar interaction, steric role
BGLU265metal ligand

site_idMCSA3
Number of Residues6
DetailsM-CSA 34
ChainResidueDetails
CHIS153metal ligand
CHIS199hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CHIS214metal ligand
CHIS246polar/non-polar interaction, steric role
CTYR255polar/non-polar interaction, steric role
CGLU265metal ligand

site_idMCSA4
Number of Residues6
DetailsM-CSA 34
ChainResidueDetails
DHIS153metal ligand
DHIS199hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
DHIS214metal ligand
DHIS246polar/non-polar interaction, steric role
DTYR255polar/non-polar interaction, steric role
DGLU265metal ligand

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PDB entries from 2024-09-11

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