3MSR

The crystal structure of an amidohydrolase from Mycoplasma synoviae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0009056	biological_process	catabolic process
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0050490	molecular_function	1,4-lactonase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 362

Chain	Residue
A	THR191
A	HOH639
A	MSE192
A	ASN218
A	ASP241
A	VAL243
A	TYR295
A	ARG299
A	HOH394
A	HOH579

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 363

Chain	Residue
A	PHE41
A	LYS217
A	LYS244
A	TYR245
A	ARG275
A	TYR278
A	HOH430
A	HOH480

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24955762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OVG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"24955762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OVG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24955762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MSR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OVG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"24955762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OVG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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