Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ORD

CRYSTALLOGRAPHIC STRUCTURE OF A PLP-DEPENDENT ORNITHINE DECARBOXYLASE FROM LACTOBACILLUS 30A TO 3.1 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004586molecular_functionornithine decarboxylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0016831molecular_functioncarboxy-lyase activity
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0004586molecular_functionornithine decarboxylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0016831molecular_functioncarboxy-lyase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 731
ChainResidue
AALA318
ATRP319
ASER352
AHIS354
ALYS355
BSER394
BTHR395
BSER396
AGLY197
ASER198
ASER199
AHIS223
ASER225
AGLN288
AASP316

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 731
ChainResidue
ASER394
ATHR395
ASER396
BGLY197
BSER198
BSER199
BHIS223
BSER225
BGLN288
BASP316
BALA318
BTRP319
BSER352
BHIS354
BLYS355

site_idPLA
Number of Residues1
Details
ChainResidue
APLP731

site_idPLB
Number of Residues1
Details
ChainResidue
BPLP731

Functional Information from PROSITE/UniProt
site_idPS00703
Number of Residues15
DetailsOKR_DC_1 Orn/Lys/Arg decarboxylases family 1 pyridoxal-P attachment site. VqSvHKqqAGfSQTS
ChainResidueDetails
AVAL350-SER364

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
AGLN356
BGLN356

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Details
ChainResidueDetails
AASP316
AHIS223
ALYS355

site_idCSA2
Number of Residues3
Details
ChainResidueDetails
BASP316
BHIS223
BLYS355

site_idMCSA1
Number of Residues3
DetailsM-CSA 860
ChainResidueDetails
ALYS224electrostatic stabiliser, steric role
ASER317electrostatic stabiliser
AGLN356covalent catalysis, proton shuttle (general acid/base)

site_idMCSA2
Number of Residues3
DetailsM-CSA 860
ChainResidueDetails
BLYS224electrostatic stabiliser, steric role
BSER317electrostatic stabiliser
BGLN356covalent catalysis, proton shuttle (general acid/base)

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon