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4MPR

Benzoylformate Decarboxylase: Is the tetramer vital for activity?

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0003984molecular_functionacetolactate synthase activity
A0009056biological_processcatabolic process
A0016831molecular_functioncarboxy-lyase activity
A0018924biological_processmandelate metabolic process
A0019596biological_processmandelate catabolic process
A0019752biological_processcarboxylic acid metabolic process
A0030976molecular_functionthiamine pyrophosphate binding
A0046872molecular_functionmetal ion binding
A0050660molecular_functionflavin adenine dinucleotide binding
A0050695molecular_functionbenzoylformate decarboxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 601
ChainResidue
AASP428
AASN455
ATHR457
ATPP602
AHOH726

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE TPP A 602
ChainResidue
AHIS70
AASN77
AGLU375
ATHR377
ASER378
AGLY401
ALEU403
AGLY427
AASP428
AGLY429
ASER430
ATYR433
AASN455
ATHR457
ATYR458
AGLY459
AALA460
ACA601
AHOH746
AHOH924
AHOH962
AASN23
APRO24
AGLY25
AGLU47

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 603
ChainResidue
AGLU37
AASP364
AHOH780
AHOH853
AHOH886
AHOH936
AHOH1232
AHOH1269

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 604
ChainResidue
AALA196
AARG294
AILE296
AASP312
AHOH802
AHOH1057
AHOH1164

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 605
ChainResidue
AGLU417
AARG420
AHOH729
AHOH945
AHOH1157

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 606
ChainResidue
AASN117
AASN117
ALEU118
ALEU118
AARG120
AARG120

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 607
ChainResidue
ALEU43
AGLN443
AGLY475
ALEU476
AASP477
AHOH1055
AHOH1060
AHOH1092

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 608
ChainResidue
AARG184
AASP187

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 609
ChainResidue
AGLY105
AGLU141
AHOH857
AHOH894
AHOH897
AHOH925

Functional Information from PROSITE/UniProt
site_idPS00187
Number of Residues20
DetailsTPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGvqlaePerqvIaViGDGS
ChainResidueDetails
AILE411-SER430

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASN117
ALEU118
AARG120
AASP428
AASN455
ATHR457

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 220
ChainResidueDetails
AGLY25electrostatic stabiliser, hydrogen bond donor
ASER26electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AGLU28electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU47hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS70electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AHIS281hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLY401electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-09-11

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