4MMG

crystal structure of YafQ mutant H87Q from E.coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003723	molecular_function	RNA binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004521	molecular_function	RNA endonuclease activity
A	0005515	molecular_function	protein binding
A	0006351	biological_process	DNA-templated transcription
A	0006402	biological_process	mRNA catabolic process
A	0006415	biological_process	translational termination
A	0016787	molecular_function	hydrolase activity
A	0016892	molecular_function	RNA endonuclease activity producing 3'-phosphomonoesters, hydrolytic mechanism
A	0040008	biological_process	regulation of growth
A	0043022	molecular_function	ribosome binding
A	0044010	biological_process	single-species biofilm formation
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0046677	biological_process	response to antibiotic
B	0003677	molecular_function	DNA binding
B	0003723	molecular_function	RNA binding
B	0004518	molecular_function	nuclease activity
B	0004519	molecular_function	endonuclease activity
B	0004521	molecular_function	RNA endonuclease activity
B	0005515	molecular_function	protein binding
B	0006351	biological_process	DNA-templated transcription
B	0006402	biological_process	mRNA catabolic process
B	0006415	biological_process	translational termination
B	0016787	molecular_function	hydrolase activity
B	0016892	molecular_function	RNA endonuclease activity producing 3'-phosphomonoesters, hydrolytic mechanism
B	0040008	biological_process	regulation of growth
B	0043022	molecular_function	ribosome binding
B	0044010	biological_process	single-species biofilm formation
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0046677	biological_process	response to antibiotic

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 101

Chain	Residue
A	HIS50
A	HIS63
A	GLN87
A	HOH221
A	HOH291
A	HOH385
B	HIS23

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 102

Chain	Residue
A	HOH202
A	HOH236
A	HOH245
A	HOH283
A	HOH309
A	HOH335
A	HOH376
B	HOH251
A	ARG22
A	ALA89

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 103

Chain	Residue
A	ARG80
A	GLU82
A	HOH215
A	HOH217
A	HOH314
A	HOH375

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 B 101

Chain	Residue
A	HIS23
B	HIS50
B	HIS63
B	HOH216
B	HOH253
B	HOH307
B	HOH365
B	HOH389
B	HOH426
B	HOH437

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 102

Chain	Residue
B	ARG80
B	GLU82
B	HOH233
B	HOH249

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 103

Chain	Residue
A	HOH318
B	ARG22
B	ALA89
B	HOH206
B	HOH290
B	HOH312
B	HOH316
B	HOH321
B	HOH420

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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