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6LDR

Structure of a K245A mutant of a Group II PLP dependent decarboxylase from Methanocaldococcus jannaschii, in complex with PLP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004068molecular_functionaspartate 1-decarboxylase activity
A0004837molecular_functiontyrosine decarboxylase activity
A0015937biological_processcoenzyme A biosynthetic process
A0016830molecular_functioncarbon-carbon lyase activity
A0016831molecular_functioncarboxy-lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0030170molecular_functionpyridoxal phosphate binding
A2001120biological_processmethanofuran biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue PLP A 401
ChainResidue
AMET37
AASP242
AHIS244
ATHR285
AHOH506
AHOH511
AHOH522
AHOH682
AGLY93
AGLY94
ATHR95
AASN98
AHIS132
ATHR181
AASP206
AALA208

site_idAC2
Number of Residues4
Detailsbinding site for residue NH4 A 402
ChainResidue
ASER36
AASN56
AASP59
AHOH647

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 403
ChainResidue
AASP260
AGLY262
ATYR263

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 404
ChainResidue
ALYS112
ALEU117
ASER118
AASN120
AASP170
AVAL171
AASP172

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 405
ChainResidue
AASN316
ALYS379
AARG380
AHOH501
AHOH505

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|Ref.4
ChainResidueDetails
AALA245

220113

PDB entries from 2024-05-22

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