6XLR

The 1.23 Angstrom crystal structure of galactose oxidase variant with genetically incorporated Cl2-Tyr272

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016491	molecular_function	oxidoreductase activity
A	0045480	molecular_function	galactose oxidase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue CU A 1001

Chain	Residue
A	PHE227
A	CYS228
A	2LT272
A	TYR495
A	HIS496
A	HIS581
A	HOH1202

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 1002

Chain	Residue
A	ASN34
A	THR37
A	ALA141
A	GLU142
A	LYS29
A	ASP32

---

site_id	AC3
Number of Residues	9
Details	binding site for residue ACT A 1003

Chain	Residue
A	ARG371
A	ALA378
A	THR398
A	PHE399
A	GLY400
A	ASN413
A	ALA414
A	HIS415
A	HOH1294

---

site_id	AC4
Number of Residues	9
Details	binding site for residue ACT A 1004

Chain	Residue
A	LEU184
A	THR204
A	SER206
A	ARG217
A	TYR253
A	ASP258
A	TRP260
A	HOH1112
A	HOH1146

---

site_id	AC5
Number of Residues	8
Details	binding site for residue ACT A 1005

Chain	Residue
A	TRP340
A	VAL392
A	LYS393
A	GLY394
A	LEU419
A	GLY420
A	HOH1159
A	HOH1261

---

site_id	AC6
Number of Residues	4
Details	binding site for residue ACT A 1006

Chain	Residue
A	ARG84
A	THR130
A	GLU131
A	ALA132

---

site_id	AC7
Number of Residues	9
Details	binding site for residue GOL A 1007

Chain	Residue
A	PRO591
A	LEU592
A	THR593
A	GLN605
A	PRO607
A	HOH1109
A	HOH1193
A	HOH1324
A	HOH1546

---

site_id	AC8
Number of Residues	6
Details	binding site for residue GOL A 1008

Chain	Residue
A	GLY157
A	LEU158
A	GLY159
A	ARG160
A	ASN531
A	TYR534

---

site_id	AC9
Number of Residues	8
Details	binding site for residue GOL A 1009

Chain	Residue
A	TYR484
A	GLN486
A	ASN531
A	HOH1122
A	HOH1246
A	HOH1284
A	HOH1308
A	HOH1401

---

site_id	AD1
Number of Residues	8
Details	binding site for residue GOL A 1010

Chain	Residue
A	PHE295
A	GLU296
A	ASN298
A	PRO313
A	HOH1213
A	HOH1319
A	HOH1491
A	HOH1629

---

site_id	AD2
Number of Residues	4
Details	binding site for residue GOL A 1011

Chain	Residue
A	TYR88
A	VAL127
A	HOH1117
A	HOH1156

---

site_id	AD3
Number of Residues	8
Details	binding site for residue GOL A 1012

Chain	Residue
A	GLY162
A	PRO163
A	ARG506
A	ILE527
A	THR529
A	HOH1126
A	HOH1189
A	HOH1715

---

site_id	AD4
Number of Residues	9
Details	binding site for residue GOL A 1013

Chain	Residue
A	ALA1
A	ASP108
A	THR110
A	THR111
A	LYS112
A	ASN191
A	ASP192
A	PHE523
A	HOH1622

---

site_id	AD5
Number of Residues	9
Details	binding site for residue GOL A 1014

Chain	Residue
A	TYR436
A	TYR484
A	LYS485
A	HOH1178
A	HOH1183
A	LEU158
A	ASN314
A	GLY363
A	ASP364

---

site_id	AD6
Number of Residues	4
Details	binding site for residue GOL A 1015

Chain	Residue
A	TYR358
A	ASP364
A	LYS485
A	HOH1632

---

site_id	AD7
Number of Residues	7
Details	binding site for residue GOL A 1016

Chain	Residue
A	PRO469
A	VAL470
A	PHE471
A	THR472
A	HOH1170
A	HOH1501
A	HOH1562

---

site_id	AD8
Number of Residues	9
Details	binding site for residue GOL A 1017

Chain	Residue
A	GLU195
A	ALA323
A	ASP324
A	LYS325
A	CYS515
A	GLY516
A	ASP517
A	HOH1172
A	HOH1704

---

site_id	AD9
Number of Residues	2
Details	binding site for residue GOL A 1018

Chain	Residue
A	THR179
A	HOH1125

---

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DGNQNGWIGrhEV

Chain	Residue	Details
A	ASP75-VAL87

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	147
Details	Domain: {"description":"F5/8 type C","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	45
Details	Repeat: {"description":"Kelch 1"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	49
Details	Repeat: {"description":"Kelch 3"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	54
Details	Repeat: {"description":"Kelch 4"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	52
Details	Repeat: {"description":"Kelch 5"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1997","firstPage":"327","lastPage":"335","volume":"2","journal":"J. Biol. Inorg. Chem.","title":"Structure and mechanism of galactose oxidase: catalytic role of tyrosine 495.","authors":["Reynolds M.P.","Baron A.J.","Wilmot C.M.","Vinecombe E.","Stevens C.","Phillips S.E.V.","Knowles P.F.","McPherson M.J."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/s007750050139"}]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Cross-link: {"description":"3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 322

Chain	Residue	Details
A	CYS228	activator, covalently attached, metal ligand
A	2LT272	activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
A	VAL294	activator, radical stabiliser
A	SER499	activator, metal ligand, proton acceptor, proton donor
A	LEU500	metal ligand
A	THR585	metal ligand

---