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1M0N

Structure of Dialkylglycine Decarboxylase Complexed with 1-Aminocyclopentanephosphonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0008483molecular_functiontransaminase activity
A0009436biological_processglyoxylate catabolic process
A0016829molecular_functionlyase activity
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 Residues6
DetailsBINDING SITE FOR RESIDUE K A 435
ChainResidue
ALEU78
ASER80
ATHR303
AVAL305
AASP307
AHOH473

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 436
ChainResidue
ALEU102
AALA95
ATHR98
APRO99

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HCP A 434
ChainResidue
AGLN52
AMET53
AGLY111
AALA112
AASN115
ATRP138
AHIS139
AGLU210
ASER215
AASP243
AGLN246
ALYS272
ATYR301
ATHR302
ATHR303
AARG406
AHOH448
AHOH451
AHOH481
AHOH498
AHOH515
AHOH564
AHOH591
AHOH592

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
ALYS272

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 482
ChainResidueDetails
ATRP138steric role
AGLU210steric role, transition state stabiliser
AASP243electrostatic stabiliser, increase electrophilicity
AGLN246electrostatic stabiliser
ALYS272covalent catalysis, proton shuttle (general acid/base)
AARG406steric role, transition state stabiliser

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PDB entries from 2024-04-24

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