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6N2H

Structure of D-ornithine/D-lysine decarboxylase from Salmonella typhimurium

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008836molecular_functiondiaminopimelate decarboxylase activity
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016830molecular_functioncarbon-carbon lyase activity
A0016831molecular_functioncarboxy-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue DMS A 501
ChainResidue
AGLY34

site_idAC2
Number of Residues6
Detailsbinding site for residue DMS A 502
ChainResidue
AGLU227
ALYS231
AGLU294
ALYS297
AHOH652
AHOH997

site_idAC3
Number of Residues3
Detailsbinding site for residue DIO A 503
ChainResidue
AHOH931
AARG22
AHOH857

site_idAC4
Number of Residues9
Detailsbinding site for residue DIO A 504
ChainResidue
ATYR9
ALEU12
AASP267
ATYR279
ATYR365
AHOH669
AHOH692
AHOH732
AHOH816

site_idAC5
Number of Residues4
Detailsbinding site for residue DIO A 505
ChainResidue
ATYR209
AGLU343
ALYS345
AHOH756

site_idAC6
Number of Residues3
Detailsbinding site for residue DIO A 506
ChainResidue
AASP388
ATYR422
ATYR430

site_idAC7
Number of Residues3
Detailsbinding site for residue DIO A 507
ChainResidue
ATHR447
AARG448
AHOH966

site_idAC8
Number of Residues6
Detailsbinding site for residue DIO A 508
ChainResidue
AALA41
ATYR44
APRO45
ATHR46
AGLU322
AHOH862

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:B4XMC6
ChainResidueDetails
ACYS387

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:B4XMC6
ChainResidueDetails
AGLY259
AGLU307
ATYR422

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:B4XMC6
ChainResidueDetails
ALLP80

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PDB entries from 2024-07-24

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