Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2E89

Crystal structure of Aquifex aeolicus TilS in a complex with ATP, Magnesium ion, and L-lysine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0016874molecular_functionligase activity
A0016879molecular_functionligase activity, forming carbon-nitrogen bonds
A0032267molecular_functiontRNA(Ile)-lysidine synthase activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0016874molecular_functionligase activity
B0016879molecular_functionligase activity, forming carbon-nitrogen bonds
B0032267molecular_functiontRNA(Ile)-lysidine synthase activity
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006400biological_processtRNA modification
C0008033biological_processtRNA processing
C0016874molecular_functionligase activity
C0016879molecular_functionligase activity, forming carbon-nitrogen bonds
C0032267molecular_functiontRNA(Ile)-lysidine synthase activity
D0000166molecular_functionnucleotide binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006400biological_processtRNA modification
D0008033biological_processtRNA processing
D0016874molecular_functionligase activity
D0016879molecular_functionligase activity, forming carbon-nitrogen bonds
D0032267molecular_functiontRNA(Ile)-lysidine synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 601
ChainResidue
CASP36
CALA132
CHIS134
CASP137
CATP902
CHOH932

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LYS B 950
ChainResidue
BVAL189
BASP191
BVAL35
BLYS182
BTRP188

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ATP A 900
ChainResidue
AALA30
APHE31
ASER32
AALA59
APHE61
AARG110
AARG113
ATHR131
AALA132
AHIS133
AARG201

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP B 901
ChainResidue
BALA30
BPHE31
BSER32
BALA59
BHIS60
BPHE61
BARG110
BARG113
BTHR131
BALA132
BHIS133
BARG201

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP C 902
ChainResidue
CALA30
CPHE31
CSER32
CALA59
CHIS60
CPHE61
CARG110
CARG113
CTHR131
CALA132
CHIS133
CMG601

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP D 903
ChainResidue
DALA30
DPHE31
DSER32
DASP36
DALA59
DHIS60
DPHE61
DARG113
DTHR131
DALA132
DHIS133
DARG201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01161
ChainResidueDetails
ASER32
BSER32
CSER32
DSER32

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
AARG110
AASP137

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
BARG110
BASP137

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
CARG110
CASP137

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kp2
ChainResidueDetails
DARG110
DASP137

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon