Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KH2

Crystal structure of the P1 bacteriophage Doc toxin (F68S) in complex with the Phd antitoxin (L17M/V39A). Northeast Structural Genomics targets ER385-ER386

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0006338	biological_process	chromatin remodeling
A	0006417	biological_process	regulation of translation
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0039604	biological_process	symbiont-mediated suppression of host translation
A	0044024	molecular_function	histone H2AS1 kinase activity
A	0044696	biological_process	killing by virus of host cell by post-segregational killing
A	0106310	molecular_function	protein serine kinase activity
B	0003677	molecular_function	DNA binding
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0006338	biological_process	chromatin remodeling
B	0006417	biological_process	regulation of translation
B	0016301	molecular_function	kinase activity
B	0016310	biological_process	phosphorylation
B	0039604	biological_process	symbiont-mediated suppression of host translation
B	0044024	molecular_function	histone H2AS1 kinase activity
B	0044696	biological_process	killing by virus of host cell by post-segregational killing
B	0106310	molecular_function	protein serine kinase activity
C	0003677	molecular_function	DNA binding
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0006338	biological_process	chromatin remodeling
C	0006417	biological_process	regulation of translation
C	0016301	molecular_function	kinase activity
C	0016310	biological_process	phosphorylation
C	0039604	biological_process	symbiont-mediated suppression of host translation
C	0044024	molecular_function	histone H2AS1 kinase activity
C	0044696	biological_process	killing by virus of host cell by post-segregational killing
C	0106310	molecular_function	protein serine kinase activity
D	0003677	molecular_function	DNA binding
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0006338	biological_process	chromatin remodeling
D	0006417	biological_process	regulation of translation
D	0016301	molecular_function	kinase activity
D	0016310	biological_process	phosphorylation
D	0039604	biological_process	symbiont-mediated suppression of host translation
D	0044024	molecular_function	histone H2AS1 kinase activity
D	0044696	biological_process	killing by virus of host cell by post-segregational killing
D	0106310	molecular_function	protein serine kinase activity
E	0001217	molecular_function	DNA-binding transcription repressor activity
E	0003677	molecular_function	DNA binding
E	0005515	molecular_function	protein binding
E	0032993	cellular_component	protein-DNA complex
E	0042803	molecular_function	protein homodimerization activity
E	0043565	molecular_function	sequence-specific DNA binding
E	0045892	biological_process	negative regulation of DNA-templated transcription
E	0097351	molecular_function	toxin sequestering activity
F	0001217	molecular_function	DNA-binding transcription repressor activity
F	0003677	molecular_function	DNA binding
F	0005515	molecular_function	protein binding
F	0032993	cellular_component	protein-DNA complex
F	0042803	molecular_function	protein homodimerization activity
F	0043565	molecular_function	sequence-specific DNA binding
F	0045892	biological_process	negative regulation of DNA-templated transcription
F	0097351	molecular_function	toxin sequestering activity
G	0001217	molecular_function	DNA-binding transcription repressor activity
G	0003677	molecular_function	DNA binding
G	0005515	molecular_function	protein binding
G	0032993	cellular_component	protein-DNA complex
G	0042803	molecular_function	protein homodimerization activity
G	0043565	molecular_function	sequence-specific DNA binding
G	0045892	biological_process	negative regulation of DNA-templated transcription
G	0097351	molecular_function	toxin sequestering activity
H	0001217	molecular_function	DNA-binding transcription repressor activity
H	0003677	molecular_function	DNA binding
H	0005515	molecular_function	protein binding
H	0032993	cellular_component	protein-DNA complex
H	0042803	molecular_function	protein homodimerization activity
H	0043565	molecular_function	sequence-specific DNA binding
H	0045892	biological_process	negative regulation of DNA-templated transcription
H	0097351	molecular_function	toxin sequestering activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 1001

Chain	Residue
A	ALA71
A	LYS73
A	ARG74

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 2001

Chain	Residue
B	TYR45
C	ARG64
D	GLU47

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE HED A 1002

Chain	Residue
D	ARG38
D	ARG42
A	ARG42
A	TYR45
A	GLU46

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE HED B 1001

Chain	Residue
B	ARG38
B	ARG42
B	VAL111
C	ARG38
C	ARG42

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 4003

Chain	Residue
E	GLN2
E	GLU25
E	VAL26
E	GLU27
E	VAL37

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 4001

Chain	Residue
F	GLN2
F	GLU25
F	VAL26
F	GLU27
F	VAL37

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 G 4002

Chain	Residue
G	GLN2
G	GLU25
G	VAL26
G	GLU27
H	GLU45

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL H 2003

Chain	Residue
H	ASP53

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 H 4004

Chain	Residue
H	GLN2
H	GLU25
H	VAL26
H	GLU27

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)