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3WWN

Crystal structure of LysZ from Thermus thermophilus complex with LysW

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009085biological_processlysine biosynthetic process
A0016301molecular_functionkinase activity
A0019878biological_processlysine biosynthetic process via aminoadipic acid
A0043744molecular_functionN2-acetyl-L-aminoadipate kinase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ALYS5
AHOH518
AGLY8
AGLY36
AGLY37
ASER38
ATYR78
AHOH456
AHOH506
AHOH515

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 101
ChainResidue
BCYS5
BCYS8
BCYS25
BCYS28

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

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
ALYS5
ALYS231

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PDB entries from 2024-07-24

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