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

3W1I

Crystal structure of the N-terminal truncated selenocysteine synthase SelA

Functional Information from GO Data
ChainGOidnamespacecontents
A0001514biological_processselenocysteine incorporation
A0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
A0005737cellular_componentcytoplasm
B0001514biological_processselenocysteine incorporation
B0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
B0005737cellular_componentcytoplasm
C0001514biological_processselenocysteine incorporation
C0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
C0005737cellular_componentcytoplasm
D0001514biological_processselenocysteine incorporation
D0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
D0005737cellular_componentcytoplasm
E0001514biological_processselenocysteine incorporation
E0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
E0005737cellular_componentcytoplasm
F0001514biological_processselenocysteine incorporation
F0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
F0005737cellular_componentcytoplasm
G0001514biological_processselenocysteine incorporation
G0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
G0005737cellular_componentcytoplasm
H0001514biological_processselenocysteine incorporation
H0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
H0005737cellular_componentcytoplasm
I0001514biological_processselenocysteine incorporation
I0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
I0005737cellular_componentcytoplasm
J0001514biological_processselenocysteine incorporation
J0004125molecular_functionL-seryl-tRNA(Sec) selenium transferase activity
J0005737cellular_componentcytoplasm
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PT A 4001
ChainResidue
AMSE65
DMSE65

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PT A 4002
ChainResidue
AMSE61

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K B 2001
ChainResidue
AASN140
BASN140
BASP317

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K C 501
ChainResidue
DASP317
CASN140
CASP317
DASN140

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K E 501
ChainResidue
EASN140
EASP317
FASN140
FASP317

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K H 501
ChainResidue
GASN140
HASN140
HASP317

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K I 501
ChainResidue
IASN140
IASP317
JASN140
JASP317

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00423
ChainResidueDetails
ALLP285
JLLP285
BLLP285
CLLP285
DLLP285
ELLP285
FLLP285
GLLP285
HLLP285
ILLP285

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon