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

6QKY

Tryptophan synthase subunit alpha from Streptococcus pneumoniae with 3D domain swap in the core of TIM barrel

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0004834molecular_functiontryptophan synthase activity
A0006568biological_processtryptophan metabolic process
A0016829molecular_functionlyase activity
B0000162biological_processtryptophan biosynthetic process
B0004834molecular_functiontryptophan synthase activity
B0006568biological_processtryptophan metabolic process
B0016829molecular_functionlyase activity
C0000162biological_processtryptophan biosynthetic process
C0004834molecular_functiontryptophan synthase activity
C0006568biological_processtryptophan metabolic process
C0016829molecular_functionlyase activity
D0000162biological_processtryptophan biosynthetic process
D0004834molecular_functiontryptophan synthase activity
D0006568biological_processtryptophan metabolic process
D0016829molecular_functionlyase activity
E0000162biological_processtryptophan biosynthetic process
E0004834molecular_functiontryptophan synthase activity
E0006568biological_processtryptophan metabolic process
E0016829molecular_functionlyase activity
F0000162biological_processtryptophan biosynthetic process
F0004834molecular_functiontryptophan synthase activity
F0006568biological_processtryptophan metabolic process
F0016829molecular_functionlyase activity
G0000162biological_processtryptophan biosynthetic process
G0004834molecular_functiontryptophan synthase activity
G0006568biological_processtryptophan metabolic process
G0016829molecular_functionlyase activity
H0000162biological_processtryptophan biosynthetic process
H0004834molecular_functiontryptophan synthase activity
H0006568biological_processtryptophan metabolic process
H0016829molecular_functionlyase activity
I0000162biological_processtryptophan biosynthetic process
I0004834molecular_functiontryptophan synthase activity
I0006568biological_processtryptophan metabolic process
I0016829molecular_functionlyase activity
J0000162biological_processtryptophan biosynthetic process
J0004834molecular_functiontryptophan synthase activity
J0006568biological_processtryptophan metabolic process
J0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue GOL A 301
ChainResidue
ALYS8

site_idAC2
Number of Residues4
Detailsbinding site for residue ACY A 302
ChainResidue
AASP63
AMSE100
ATYR175
BGLU52

site_idAC3
Number of Residues3
Detailsbinding site for residue PEG B 301
ChainResidue
BGLU38
BTHR39
BHOH410

site_idAC4
Number of Residues7
Detailsbinding site for residue ACY B 302
ChainResidue
BASP63
BILE67
BMSE100
BTYR175
BGLY233
CLYS185
AGLU52

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL C 301
ChainResidue
CGLU86
CLYS89
CASP117

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL C 302
ChainResidue
CGLU38
CPHE42
DHOH403

site_idAC7
Number of Residues5
Detailsbinding site for residue ACY C 303
ChainResidue
CASP63
CMSE100
CTYR175
CGLY233
DGLU52

site_idAC8
Number of Residues3
Detailsbinding site for residue ACY D 301
ChainResidue
CGLU52
DASP63
DTYR175

site_idAC9
Number of Residues1
Detailsbinding site for residue PEG E 301
ChainResidue
ELYS116

site_idAD1
Number of Residues4
Detailsbinding site for residue ACY E 302
ChainResidue
EILE67
EMSE100
ETYR175
FGLU52

site_idAD2
Number of Residues3
Detailsbinding site for residue ACY E 303
ChainResidue
EGLU52
FILE67
FTYR175

site_idAD3
Number of Residues4
Detailsbinding site for residue ACY G 301
ChainResidue
GMSE100
GTYR175
GHOH408
HGLU52

site_idAD4
Number of Residues4
Detailsbinding site for residue ACY H 301
ChainResidue
GGLU52
HASP63
HTYR175
HGLY233

site_idAD5
Number of Residues4
Detailsbinding site for residue ACY I 301
ChainResidue
IASP63
IMSE100
ITYR175
JGLU52

site_idAD6
Number of Residues5
Detailsbinding site for residue ACY J 301
ChainResidue
IGLU52
JILE67
JMSE100
JTYR175
JHOH420

Functional Information from PROSITE/UniProt
site_idPS00167
Number of Residues14
DetailsTRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. IEVGiPFSDPVADG
ChainResidueDetails
AILE51-GLY64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00131
ChainResidueDetails
AGLU52
EASP63
FGLU52
FASP63
GGLU52
GASP63
HGLU52
HASP63
IGLU52
IASP63
JGLU52
AASP63
JASP63
BGLU52
BASP63
CGLU52
CASP63
DGLU52
DASP63
EGLU52

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon