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3WWM

Crystal structure of LysZ from Thermus thermophilus with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003991molecular_functionacetylglutamate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006526biological_processarginine biosynthetic process
A0009085biological_processlysine biosynthetic process
A0016301molecular_functionkinase activity
A0019878biological_processlysine biosynthetic process via aminoadipic acid
A0043744molecular_functionN2-acetyl-L-aminoadipate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP A 301
ChainResidue
ALYS5
AARG230
AHOH401
AHOH427
AGLY7
AGLY8
AGLY36
AGLY37
ASER38
ATYR78
ATYR200
AMET228

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:25392000, ECO:0007744|PDB:3WWM
ChainResidueDetails
ATYR78
ALYS5

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02082
ChainResidueDetails
AARG64
AASN168

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_02082
ChainResidueDetails
ALYS231
ALYS5

220472

PDB entries from 2024-05-29

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