6MFZ

Crystal structure of dimodular LgrA in a condensation state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0009058	biological_process	biosynthetic process
A	0031177	molecular_function	phosphopantetheine binding
B	0003824	molecular_function	catalytic activity
B	0009058	biological_process	biosynthetic process
B	0031177	molecular_function	phosphopantetheine binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue PNS A 1901

Chain	Residue
A	ILE796
A	ASP1096
A	ARG1106
A	SER1760

---

site_id	AC2
Number of Residues	3
Details	binding site for residue PNS A 1902

Chain	Residue
A	SER729
A	TYR748
A	TYR1015

---

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. ELGGDSIKGLQIASRL

Chain	Residue	Details
A	GLU1755-LEU1770

---

site_id	PS00455
Number of Residues	12
Details	AMP_BINDING Putative AMP-binding domain signature. VMYTSGSTGlAK

Chain	Residue	Details
A	VAL348-LYS359
A	VAL1366-LYS1377

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	74
Details	Domain: {"description":"Carrier 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	74
Details	Domain: {"description":"Carrier 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---