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1P4C

High Resolution Structure of Oxidized Active Mutant of (S)-Mandelate Dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
ATYR131
AHOH1276
AARG165
AHIS255
AARG258
AGLN259
AFMN490
AHOH1011
AHOH1043
AHOH1070

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FMN A 490
ChainResidue
ATYR26
APRO79
ATHR80
AGLY81
ASER108
AGLN129
ATYR131
ATHR156
ALYS231
ASER253
AHIS255
AGLY256
AARG258
AASP284
ASER285
AGLY286
AARG288
AGLY307
AARG308
ASO4901
AHOH903
AHOH905
AHOH913
AHOH943
AHOH1097

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 890
ChainResidue
ATRP87
ALYS89
AASP240
AILE243
ALYS276
ATHR277
AHOH1065
AHOH1074
AHOH1163

Functional Information from PROSITE/UniProt
site_idPS00557
Number of Residues7
DetailsFMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ
ChainResidueDetails
ASER253-GLN259

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683
ChainResidueDetails
AHIS255

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:19465768, ECO:0007744|PDB:2A85
ChainResidueDetails
ATYR26
ATYR131
AARG165
AHIS255
AARG258

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:14604988, ECO:0000269|PubMed:30071260, ECO:0007744|PDB:1P4C, ECO:0007744|PDB:6BFG
ChainResidueDetails
APRO79
ASER108
AGLN129
ATHR156
ALYS231
AASP284
AGLY307

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
ATYR131
AASP158
AHIS255
AARG258
ATYR26

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
ATYR131
AHIS255
AARG258
AASP158

site_idMCSA1
Number of Residues5
DetailsM-CSA 852
ChainResidueDetails
ASER108electrostatic stabiliser
ATYR131electrostatic stabiliser, modifies pKa
ATHR156electrostatic stabiliser
ALYS231electrostatic stabiliser, enhance reactivity
AHIS255proton shuttle (general acid/base)

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PDB entries from 2025-06-18

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