1XEM

High Resolution Crystal Structure of Escherichia coli Zinc- Peptide Deformylase bound to formate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0008198	molecular_function	ferrous iron binding
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0031365	biological_process	N-terminal protein amino acid modification
A	0042586	molecular_function	peptide deformylase activity
A	0043022	molecular_function	ribosome binding
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 401

Chain	Residue
A	GLN50
A	CYS90
A	HIS132
A	HIS136
A	FMT501

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT A 501

Chain	Residue
A	HIS132
A	GLU133
A	HIS136
A	ZN401
A	GLY45
A	GLN50
A	CYS90
A	LEU91

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT A 502

Chain	Residue
A	ARG69
A	VAL71
A	ARG113
A	FMT505
A	HOH519
A	HOH562
A	HOH572
A	HOH630
A	HOH644

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 503

Chain	Residue
A	GLN131
A	MET134
A	FMT509
A	HOH546
A	HOH590
A	HOH596
A	HOH736

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 504

Chain	Residue
A	ILE8
A	PRO9
A	ASP10
A	ARG14
A	HOH671
A	HOH674
A	HOH718

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 505

Chain	Residue
A	ASP112
A	ASP114
A	FMT502
A	HOH562
A	HOH630
A	HOH683

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 506

Chain	Residue
A	LYS80
A	SER81
A	HOH580
A	HOH637
A	HOH707
A	HOH707

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT A 507

Chain	Residue
A	LYS80
A	GLU83
A	FMT509
A	HOH574
A	HOH594
A	HOH596
A	HOH669
A	HOH726
A	HOH736

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 508

Chain	Residue
A	HIS7
A	GLU41
A	HOH575
A	HOH748
A	HOH786

---

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FMT A 509

Chain	Residue
A	GLN131
A	ASP135
A	TYR145
A	FMT503
A	FMT507
A	HOH521
A	HOH574
A	HOH669

---

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT A 510

Chain	Residue
A	GLU95
A	GLN96
A	LYS157
A	HOH545
A	HOH577
A	HOH716
A	HOH734

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PubMed","id":"9846875","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9846875","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
A	GLU133
A	GLY45
A	LEU91
A	GLN50

---

site_id	MCSA1
Number of Residues	7
Details	M-CSA 98

Chain	Residue	Details
A	GLY45	activator, hydrogen bond acceptor
A	GLN50	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	CYS90	metal ligand
A	LEU91	electrostatic stabiliser, hydrogen bond donor
A	HIS132	metal ligand
A	GLU133	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS136	metal ligand

---