5T9C

Crystal structure of B. subtilis 168 GlpQ in complex with glycerol-3-phosphate (1 hour soak)

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CA E 301

Chain	Residue
E	GLU70
E	ASP72
E	GLU152
E	G3P302
E	HOH429

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site_id	AC2
Number of Residues	14
Details	binding site for residue G3P E 302

Chain	Residue
E	HIS85
E	GLU152
E	LYS154
E	GLN188
E	LEU210
E	TYR259
E	PHE279
E	CA301
E	HOH448
E	HOH472
E	HIS43
E	ARG44
E	GLU70
E	ASP72

---

site_id	AC3
Number of Residues	6
Details	binding site for residue PO4 E 303

Chain	Residue
E	HIS43
E	THR260
E	ASN262
E	ASN281
E	HOH432
E	HOH448

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site_id	AC4
Number of Residues	6
Details	binding site for residue NA E 304

Chain	Residue
E	ASP90
E	THR93
E	HOH414
E	HOH514
E	HOH536
E	HOH541

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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
E	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
E	HIS85

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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
E	HIS43
E	ARG44
E	GLU70
E	ASP72
E	HIS85
E	GLU152
E	GLN188

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