5XPF

High-resolution X-ray structure of the T26H mutant of T4 lysozyme

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	4
Details	binding site for residue NA A 201

Chain	Residue
A	TYR25
A	PRO37
A	HOH432
A	HOH471

---

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

Chain	Residue
A	GLY30
A	PHE104
A	HOH403
A	HOH443
A	HOH480

---

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

Chain	Residue
A	GLU11
A	HOH386
A	HOH408
A	HOH418
A	HOH483
A	HOH509

---

site_id	AC4
Number of Residues	3
Details	binding site for residue CL A 204

Chain	Residue
A	HIS31
A	ALA49
A	LYS135

---

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

Chain	Residue
A	ASN132
A	LYS135
A	HOH394

---

site_id	AC6
Number of Residues	2
Details	binding site for residue CL A 206

Chain	Residue
A	ASN81
A	ALA82

---

site_id	AC7
Number of Residues	8
Details	binding site for residue CL A 207

Chain	Residue
A	SER90
A	LYS124
A	THR142
A	PRO143
A	ASN144
A	ARG145
A	HOH342
A	HOH531

---

site_id	AC8
Number of Residues	2
Details	binding site for residue CL A 208

Chain	Residue
A	HOH327
A	HOH359

---

site_id	AC9
Number of Residues	6
Details	binding site for residue HEZ A 209

Chain	Residue
A	THR34
A	SER36
A	GLU45
A	ASN116
A	ARG119
A	HOH420

---

site_id	AD1
Number of Residues	9
Details	binding site for residue HEZ A 210

Chain	Residue
A	GLY51
A	MET106
A	GLY110
A	ARG137
A	TRP138
A	HOH312
A	HOH340
A	HOH380
A	HOH406

---

site_id	AD2
Number of Residues	3
Details	binding site for residue HEZ A 211

Chain	Residue
A	GLN123
A	ARG125
A	HOH329

---

site_id	AD3
Number of Residues	8
Details	binding site for residue HEZ A 212

Chain	Residue
A	LEU13
A	ARG14
A	LEU15
A	LYS16
A	TYR18
A	HOH308
A	HOH341
A	HOH527

---

site_id	AD4
Number of Residues	3
Details	binding site for residue GOL A 213

Chain	Residue
A	TYR24
A	LYS35
A	HOH482

---

site_id	AD5
Number of Residues	2
Details	binding site for residue GOL A 214

Chain	Residue
A	ARG80
A	HOH424

---

site_id	AD6
Number of Residues	6
Details	binding site for residue GOL A 215

Chain	Residue
A	ILE17
A	LYS19
A	TYR25
A	HOH303
A	HOH309
A	HOH365

---

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

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