3DPQ

Crystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form B)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity
B	0005524	molecular_function	ATP binding
B	0016887	molecular_function	ATP hydrolysis activity
C	0002376	biological_process	immune system process
C	0005576	cellular_component	extracellular region
C	0042742	biological_process	defense response to bacterium
C	0045087	biological_process	innate immune response
D	0002376	biological_process	immune system process
D	0005576	cellular_component	extracellular region
D	0042742	biological_process	defense response to bacterium
D	0045087	biological_process	innate immune response
E	0005524	molecular_function	ATP binding
E	0016887	molecular_function	ATP hydrolysis activity
F	0005524	molecular_function	ATP binding
F	0016887	molecular_function	ATP hydrolysis activity
G	0002376	biological_process	immune system process
G	0005576	cellular_component	extracellular region
G	0042742	biological_process	defense response to bacterium
G	0045087	biological_process	innate immune response
H	0002376	biological_process	immune system process
H	0005576	cellular_component	extracellular region
H	0042742	biological_process	defense response to bacterium
H	0045087	biological_process	innate immune response

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 E 1001

Chain	Residue
E	ARG517
G	PRO10

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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