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2DKB

DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES

Functional Information from GO Data
ChainGOidnamespacecontents
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0008483molecular_functiontransaminase activity
A0009436biological_processglyoxylate catabolic process
A0016831molecular_functioncarboxy-lyase activity
A0019481biological_processL-alanine catabolic process, by transamination
A0030170molecular_functionpyridoxal phosphate binding
A0047432molecular_function2,2-dialkylglycine decarboxylase (pyruvate) activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 435
ChainResidue
AALA95
ATHR98
APRO99
ALEU102
AHOH526

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 436
ChainResidue
ALEU78
AVAL305
AASP307
AHOH509
AHOH519

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PLP A 437
ChainResidue
ATHR110
AGLY111
AALA112
AASN115
ATRP138
AHIS139
AGLU210
AASP243
AALA245
AGLN246
ALYS272
ATHR302
ATHR303
AMES434
AHOH536
AHOH544
AHOH552
AHOH621
AHOH625

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES A 434
ChainResidue
AGLN52
ATRP138
ASER215
AGLN246
ALYS272
AARG406
APLP437
AHOH642

site_idME1
Number of Residues4
DetailsMETAL BINDING SITE 1
ChainResidue
AALA95
ATHR98
APRO99
ALEU102

site_idME2
Number of Residues3
DetailsMETAL BINDING SITE 2
ChainResidue
ALEU78
AVAL305
AASP307

site_idPLP
Number of Residues2
DetailsRESIDUE LYS 272 HAS THE COFACTOR PYRIDOXAL-5'-PHOSPHATE COVALENTLY ATTACHED TO IT
ChainResidue
ALYS272
APLP437

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDEAqt.GVgRtGtmfacqrdgvtp....DILtlSKtlgAG
ChainResidueDetails
ALEU240-GLY277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ATHR273

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 482
ChainResidueDetails
AHIS139steric role
APRO211steric role, transition state stabiliser
AGLU244electrostatic stabiliser, increase electrophilicity
ATHR247electrostatic stabiliser
ATHR273covalent catalysis, proton shuttle (general acid/base)
AILE407steric role, transition state stabiliser

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PDB entries from 2024-05-29

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