5JQJ

Directed evolutionary changes in MBL super family - NDM-1 Round 10 crystal-1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0042597	cellular_component	periplasmic space
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 301

Chain	Residue
A	HIS120
A	HIS122
A	HIS189
A	ZN302
A	HOH536

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site_id	AC2
Number of Residues	6
Details	binding site for residue ZN A 302

Chain	Residue
A	HOH433
A	HOH536
A	ASP124
A	CYS208
A	HIS250
A	ZN301

---

site_id	AC3
Number of Residues	12
Details	binding site for residue MES A 303

Chain	Residue
A	VAL73
A	ARG85
A	ASN176
A	PHE177
A	GLY178
A	ARG211
A	LYS216
A	SER217
A	HIS250
A	HOH523
A	HOH543
A	HOH600

---

site_id	AC4
Number of Residues	10
Details	binding site for residue MES A 304

Chain	Residue
A	HIS122
A	ASP124
A	ASN176
A	HIS189
A	ARG211
A	GLY219
A	ASN220
A	HOH433
A	HOH499
A	HOH536

---

site_id	AC5
Number of Residues	2
Details	binding site for residue MG A 305

Chain	Residue
A	GLU152
A	GLU223

---

site_id	AC6
Number of Residues	6
Details	binding site for residue MG A 306

Chain	Residue
A	ASP95
A	HOH426
A	HOH453
A	HOH485
A	HOH513
A	HOH635

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25815530","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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