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5XOY

Crystal structure of LysK from Thermus thermophilus in complex with Lysine

Replaces:  3X3E
Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
A0009085biological_processlysine biosynthetic process
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0019878biological_processlysine biosynthetic process via aminoadipic acid
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
B0005737cellular_componentcytoplasm
B0008270molecular_functionzinc ion binding
B0009085biological_processlysine biosynthetic process
B0016787molecular_functionhydrolase activity
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0019878biological_processlysine biosynthetic process via aminoadipic acid
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue LYS A 401
ChainResidue
AGLU124
AGLU125
AALA126
ASER129
AARG162
AARG236
ATHR300
BHIS175

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 402
ChainResidue
AGLY264
AARG265
APHE263

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 B 401
ChainResidue
BHIS221
BGLU224
BLEU225
BARG226

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 B 402
ChainResidue
BPHE263
BGLY264
BARG265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P44514, ECO:0000255|HAMAP-Rule:MF_01120
ChainResidueDetails
AASP69
BASP69

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P44514, ECO:0000255|HAMAP-Rule:MF_01120
ChainResidueDetails
AGLU124
BGLU124

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P44514, ECO:0000255|HAMAP-Rule:MF_01120
ChainResidueDetails
AHIS67
BHIS326
AASP91
AGLU125
AGLU148
AHIS326
BHIS67
BASP91
BGLU125
BGLU148

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PDB entries from 2024-07-24

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