5VNR

X-ray structure of perdeuterated T4 lysozyme cysteine-free pseudo-wild type at cryogenic temperature

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0009253	biological_process	peptidoglycan catabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue PO4 A 201

Chain	Residue
A	LYS19
A	ARG125
A	TRP126
A	ASP127
A	GLU128
A	HOH304
A	HOH408

---

site_id	AC2
Number of Residues	5
Details	binding site for residue NA A 202

Chain	Residue
A	HOH346
A	HOH372
A	HOH407
A	GLU11
A	TYR18

---

site_id	AC3
Number of Residues	6
Details	binding site for residue HED A 203

Chain	Residue
A	PHE4
A	ASP72
A	ALA93
A	ILE100
A	HOH307
A	HOH342

---

site_id	AC4
Number of Residues	5
Details	binding site for residue CL A 204

Chain	Residue
A	LYS124
A	THR142
A	ASN144
A	ARG145
A	HOH582

---

site_id	AC5
Number of Residues	3
Details	binding site for residue CL A 205

Chain	Residue
A	HIS31
A	LYS135
A	HOH424

---

site_id	AC6
Number of Residues	10
Details	binding site for residue GOL A 206

Chain	Residue
A	ASP72
A	ARG76
A	LEU79
A	ASP89
A	HOH301
A	HOH302
A	HOH307
A	HOH319
A	HOH355
A	HOH381

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098

Chain	Residue	Details
A	GLU11

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098

Chain	Residue	Details
A	ASP20

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:8266098

Chain	Residue	Details
A	LEU32
A	PHE104

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000303|PubMed:7831309

Chain	Residue	Details
A	SER117
A	ASN132

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU11	proton shuttle (general acid/base)
A	ASP20	covalent catalysis

---