4L1G

Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0046872	molecular_function	metal ion binding
B	0005975	biological_process	carbohydrate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B	0046872	molecular_function	metal ion binding
C	0005975	biological_process	carbohydrate metabolic process
C	0016787	molecular_function	hydrolase activity
C	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C	0046872	molecular_function	metal ion binding
D	0005975	biological_process	carbohydrate metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	HIS231
A	LEU232
A	GLN233
A	HOH561

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT A 302

Chain	Residue
A	TRP193
A	HIS225
A	ASP80
A	HIS135
A	PRO170
A	PXU171
A	TYR172

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 301

Chain	Residue
B	HIS231
B	LEU232
B	GLN233
B	HOH546

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ACT B 302

Chain	Residue
B	ASP80
B	ASP81
B	HIS131
B	HIS135
B	PXU171
B	TYR172
B	HIS225
B	HOH509
B	HOH583

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 301

Chain	Residue
A	ASN99
A	LYS247
C	HIS98
C	PRO244
C	LYS247
C	HOH420
C	HOH441
C	HOH463

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 302

Chain	Residue
C	HIS231
C	LEU232
C	GLN233
C	HOH454

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT C 303

Chain	Residue
C	ASP80
C	PRO170
C	PXU171
C	TYR172
C	TRP193
C	HIS225
C	HOH575

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 301

Chain	Residue
B	ASN99
B	LYS247
D	HIS98
D	ILE243
D	PRO244
D	LYS247
D	HOH425
D	HOH436
D	HOH523

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 302

Chain	Residue
D	HIS231
D	LEU232
D	GLN233
D	HOH446
D	HOH550

---

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT D 303

Chain	Residue
D	ASP80
D	ASP81
D	HIS131
D	HIS135
D	PXU171
D	TYR172
D	HIS225
D	HOH557

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01014","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01014","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2017","submissionDatabase":"PDB data bank","title":"Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide.","authors":["Fadouloglou V.E.","Kotsifaki D.","Kokkinidis M."]}}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"2-hydroxyproline; partial","evidences":[{"source":"PubMed","id":"28333455","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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