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	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0005576	cellular_component	extracellular region
C	0042742	biological_process	defense response to bacterium
C	0045087	biological_process	innate immune response
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	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0005524	molecular_function	ATP binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0005576	cellular_component	extracellular region
G	0042742	biological_process	defense response to bacterium
G	0045087	biological_process	innate immune response
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	4
Details	CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:10076062

Chain	Residue	Details
C	THR8
D	THR8
G	THR8
H	THR8
E	LYS421
E	LYS556
F	LYS421
F	LYS556

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site_id	SWS_FT_FI2
Number of Residues	12
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122

Chain	Residue	Details
A	LYS502
F	LYS502
F	LYS528
F	LYS587
A	LYS528
A	LYS587
B	LYS502
B	LYS528
B	LYS587
E	LYS502
E	LYS528
E	LYS587

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