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

5VXT

Crystal structure of catechol 1,2-dioxygenase from Burkholderia ambifaria

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0006725biological_processobsolete cellular aromatic compound metabolic process
A0008199molecular_functionferric iron binding
A0009712biological_processcatechol-containing compound metabolic process
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0018576molecular_functioncatechol 1,2-dioxygenase activity
A0019614biological_processcatechol-containing compound catabolic process
A0042952biological_processbeta-ketoadipate pathway
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0003824molecular_functioncatalytic activity
B0005506molecular_functioniron ion binding
B0006725biological_processobsolete cellular aromatic compound metabolic process
B0008199molecular_functionferric iron binding
B0009712biological_processcatechol-containing compound metabolic process
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0018576molecular_functioncatechol 1,2-dioxygenase activity
B0019614biological_processcatechol-containing compound catabolic process
B0042952biological_processbeta-ketoadipate pathway
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue PTY A 401
ChainResidue
AGLU60
BPTY401
ATYR67
AALA77
AARG220
AHOH611
AHOH710
BILE39
BLEU43
BALA77

site_idAC2
Number of Residues4
Detailsbinding site for residue FE A 402
ChainResidue
ATYR170
AHIS230
AHIS232
ACAQ403

site_idAC3
Number of Residues8
Detailsbinding site for residue CAQ A 403
ChainResidue
ALEU79
APRO114
ATYR170
AARG227
AHIS230
AHIS232
AGLN246
AFE402

site_idAC4
Number of Residues2
Detailsbinding site for residue EDO A 404
ChainResidue
APHE173
AHOH551

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 405
ChainResidue
AGLN38
AHOH540
AHOH679
AHOH727

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 406
ChainResidue
AHIS172
AGLN179
AHOH503
AHOH582

site_idAC7
Number of Residues14
Detailsbinding site for residue PTY B 401
ChainResidue
AILE39
ALEU43
ALEU44
AASP46
APTY401
BLEU43
BASP46
BGLU60
BTYR67
BGLN216
BARG220
BHOH519
BHOH593
BHOH648

site_idAC8
Number of Residues4
Detailsbinding site for residue FE B 402
ChainResidue
BTYR170
BHIS230
BHIS232
BCAQ403

site_idAC9
Number of Residues8
Detailsbinding site for residue CAQ B 403
ChainResidue
BLEU79
BPRO114
BLEU115
BTYR170
BARG227
BHIS230
BHIS232
BFE402

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO B 404
ChainResidue
BGLY148
BLEU149
BHIS240
BPRO298

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO B 405
ChainResidue
BILE255
BASP258
BTYR261
BALA262
BTHR263

Functional Information from PROSITE/UniProt
site_idPS00083
Number of Residues29
DetailsINTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. IhGtVtgldGkpVagalVECwhanshGfY
ChainResidueDetails
AILE142-TYR170

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon