5T91

Crystal structure of B. subtilis 168 GlpQ in complex with bicine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0006071	biological_process	glycerol metabolic process
A	0006629	biological_process	lipid metabolic process
A	0008081	molecular_function	phosphoric diester hydrolase activity
A	0008889	molecular_function	glycerophosphodiester phosphodiesterase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CA A 301

Chain	Residue
A	HIS43
A	GLU70
A	BCN302
A	HOH420

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site_id	AC2
Number of Residues	12
Details	binding site for residue BCN A 302

Chain	Residue
A	GLN188
A	PHE190
A	TYR259
A	PHE279
A	CA301
A	HOH420
A	HOH514
A	HIS43
A	ARG44
A	GLU70
A	ASP72
A	HIS85

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NA A 303

Chain	Residue
A	ASP90
A	THR93
A	HOH445
A	HOH534
A	HOH582
A	HOH589

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:27780866

Chain	Residue	Details
A	HIS43

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:27780866

Chain	Residue	Details
A	HIS85

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:27780866, ECO:0007744|PDB:5T9B, ECO:0007744|PDB:5T9C

Chain	Residue	Details
A	HIS43
A	ARG44
A	GLU70
A	ASP72
A	HIS85
A	GLU152
A	GLN188

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