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1D7R

CRYSTAL STRUCTURE OF THE COMPLEX OF 2,2-DIALKYLGLYCINE DECARBOXYLASE WITH 5PA

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 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 Residues20
DetailsBINDING SITE FOR RESIDUE 5PA A 500
ChainResidue
AGLN52
AGLY111
AALA112
ATRP138
AHIS139
AGLU210
ASER215
AASP243
AALA245
AGLN246
ALYS272
ATYR301
ATHR302
ATHR303
AARG406
AHOH504
AHOH511
AHOH513
AHOH602
AHOH605

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 2024-09-11

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