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

5VG3

Structure of Oxalate Decarboxylase from Bacillus subtilis at pH 4.6

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016831molecular_functioncarboxy-lyase activity
A0033609biological_processoxalate metabolic process
A0046564molecular_functionoxalate decarboxylase activity
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0016831molecular_functioncarboxy-lyase activity
B0033609biological_processoxalate metabolic process
B0046564molecular_functionoxalate decarboxylase activity
B0046872molecular_functionmetal ion binding
C0005737cellular_componentcytoplasm
C0016831molecular_functioncarboxy-lyase activity
C0033609biological_processoxalate metabolic process
C0046564molecular_functionoxalate decarboxylase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue ACT A 401
ChainResidue
AMET84
AARG92
AHIS95
AHIS97
AGLU101
ALEU153
APHE155
AMN411
AHOH523

site_idAC2
Number of Residues7
Detailsbinding site for residue ACT A 402
ChainResidue
AVAL243
AILE245
AALA260
AARG270
AGLU333
ATYR340
AHOH671

site_idAC3
Number of Residues1
Detailsbinding site for residue ACT A 403
ChainResidue
CASN219

site_idAC4
Number of Residues3
Detailsbinding site for residue ACT A 404
ChainResidue
AVAL222
APRO225
AHOH673

site_idAC5
Number of Residues6
Detailsbinding site for residue ACT A 405
ChainResidue
AGLU117
APRO135
ASER136
AHOH505
AHOH897
CPRO276

site_idAC6
Number of Residues3
Detailsbinding site for residue ACT A 406
ChainResidue
AGLY108
AGLY127
AGLU128

site_idAC7
Number of Residues6
Detailsbinding site for residue ACT A 407
ChainResidue
AGLN143
AASN204
AGLN205
AHOH659
CTHR355
CPHE356

site_idAC8
Number of Residues2
Detailsbinding site for residue ACT A 408
ChainResidue
ATYR104
AILE106

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL A 409
ChainResidue
ALYS87
AGLU146
AHOH676
AHOH788
BGLY13
BASP14
BGLY16

site_idAD1
Number of Residues6
Detailsbinding site for residue MN A 410
ChainResidue
AHIS273
AHIS275
AGLU280
AHIS319
AHOH571
AHOH577

site_idAD2
Number of Residues6
Detailsbinding site for residue MN A 411
ChainResidue
AHIS95
AHIS97
AGLU101
AHIS140
AACT401
AHOH523

site_idAD3
Number of Residues10
Detailsbinding site for residue ACT B 401
ChainResidue
BMET84
BARG92
BHIS95
BHIS97
BGLU101
BLEU153
BPHE155
BTYR200
BMN408
BHOH545

site_idAD4
Number of Residues7
Detailsbinding site for residue ACT B 402
ChainResidue
BVAL243
BILE245
BALA260
BARG270
BGLU333
BTYR340
BHOH646

site_idAD5
Number of Residues3
Detailsbinding site for residue ACT B 403
ChainResidue
BHIS56
BARG58
BASN163

site_idAD6
Number of Residues3
Detailsbinding site for residue ACT B 404
ChainResidue
BTYR104
BMET105
BILE106

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL B 405
ChainResidue
BASP41
BHIS42
BGLY43
BHOH509
BHOH631

site_idAD8
Number of Residues1
Detailsbinding site for residue GOL B 406
ChainResidue
BHIS339

site_idAD9
Number of Residues6
Detailsbinding site for residue MN B 407
ChainResidue
BHIS273
BHIS275
BGLU280
BHIS319
BHOH558
BHOH568

site_idAE1
Number of Residues6
Detailsbinding site for residue MN B 408
ChainResidue
BHIS95
BHIS97
BGLU101
BHIS140
BACT401
BHOH545

site_idAE2
Number of Residues9
Detailsbinding site for residue ACT C 401
ChainResidue
CHIS95
CHIS97
CGLU101
CLEU153
CPHE155
CMN406
CHOH523
CMET84
CARG92

site_idAE3
Number of Residues8
Detailsbinding site for residue ACT C 402
ChainResidue
CVAL243
CILE245
CALA260
CVAL262
CARG270
CGLU333
CTYR340
CHOH641

site_idAE4
Number of Residues3
Detailsbinding site for residue MPD C 403
ChainResidue
CTYR104
CILE106
CHOH763

site_idAE5
Number of Residues3
Detailsbinding site for residue MPD C 404
ChainResidue
CLYS87
CHOH511
CHOH667

site_idAE6
Number of Residues6
Detailsbinding site for residue MN C 405
ChainResidue
CHIS273
CHIS275
CGLU280
CHIS319
CHOH585
CHOH586

site_idAE7
Number of Residues6
Detailsbinding site for residue MN C 406
ChainResidue
CHIS95
CHIS97
CGLU101
CHIS140
CACT401
CHOH523

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:12056897
ChainResidueDetails
AGLU333
BGLU333
CGLU333

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:12056897
ChainResidueDetails
BHIS273
BHIS275
BGLU280
BHIS319
CHIS95
CHIS97
CGLU101
CHIS140
CHIS273
CHIS275
CGLU280
CHIS319
AHIS95
AHIS97
AGLU101
AHIS140
AHIS273
AHIS275
AGLU280
AHIS319
BHIS95
BHIS97
BGLU101
BHIS140

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 231
ChainResidueDetails
AARG92attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AHIS95metal ligand
AHIS97metal ligand
AGLU101metal ligand
AHIS140metal ligand
AGLU162electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 231
ChainResidueDetails
BARG92attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
BHIS95metal ligand
BHIS97metal ligand
BGLU101metal ligand
BHIS140metal ligand
BGLU162electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA3
Number of Residues6
DetailsM-CSA 231
ChainResidueDetails
CARG92attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
CHIS95metal ligand
CHIS97metal ligand
CGLU101metal ligand
CHIS140metal ligand
CGLU162electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon