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1D7U

Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with LCS

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 Residues4
DetailsBINDING SITE FOR RESIDUE NA A 435
ChainResidue
AALA95
ATHR98
APRO99
ALEU102

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 436
ChainResidue
AHOH529
ALEU78
ASER80
ATHR303
AVAL305
AASP307

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE LCS A 500
ChainResidue
AGLN52
ATHR110
AGLY111
AALA112
AASN115
ATRP138
AHIS139
AGLU210
ASER215
AASP243
AALA245
AGLN246
ALYS272
ATYR301
ATHR302
ATHR303
AARG406
AHOH504
AHOH511
AHOH513
AHOH602
AHOH604
AHOH605
AHOH674
AHOH675

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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