2WQ8

Glycan labelling using engineered variants of galactose oxidase obtained by directed evolution

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 1640

Chain	Residue
A	PHE227
A	CYS228
A	TYR272
A	TYR495
A	HIS496
A	HIS581
A	ACY1642

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1641

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

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY A 1642

Chain	Residue
A	TYR272
A	PHE290
A	TYR495
A	HIS496
A	CU1640

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ACY A 1643

Chain	Residue
A	ARG371
A	ALA378
A	ALA381
A	THR398
A	GLY400
A	ASN413
A	ALA414
A	HIS415
A	EDO1644

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 1644

Chain	Residue
A	ALA378
A	PRO379
A	ALA381
A	GLY400
A	GLY401
A	THR411
A	ASN413
A	ACY1643
A	HOH2375

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 1645

Chain	Residue
A	ASN385
A	ALA386
A	VAL387
A	THR443
A	SER444
A	THR582
A	GLN587
A	EDO1646
A	HOH2333

---

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EDO A 1646

Chain	Residue
A	THR443
A	SER497
A	ILE498
A	SER499
A	ALA579
A	THR580
A	HIS581
A	THR582
A	VAL583
A	EDO1645
A	HOH2376

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1647

Chain	Residue
A	ILE475
A	GLN486
A	PHE528
A	PRO530
A	ASN531
A	TYR532
A	GOL1655
A	HOH2377

---

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 1648

Chain	Residue
A	PRO72
A	TRP81
A	ILE82
A	TRP105
A	PHE106
A	ASP108
A	LYS112
A	ALA132
A	HOH2378

---

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1649

Chain	Residue
A	HIS334
A	ALA335
A	TRP336
A	GLY384
A	THR582
A	VAL583
A	HOH2379
A	HOH2380

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1650

Chain	Residue
A	LEU158
A	ASN314
A	TYR436
A	TYR484
A	LYS485

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1651

Chain	Residue
A	PRO156
A	GLY157
A	LEU158
A	GLY159
A	ARG160
A	ASN531
A	GLY538

---

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1652

Chain	Residue
A	PRO591
A	LEU592
A	THR593
A	GLN605
A	PRO607

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1653

Chain	Residue
A	PHE295
A	GLU296
A	ASN298
A	GLY299
A	SER311
A	VAL268

---

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1654

Chain	Residue
A	HIS40
A	ARG73
A	ASN79
A	HOH2015
A	HOH2381

---

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1655

Chain	Residue
A	TYR484
A	GLN486
A	ASN531
A	EDO1647
A	HOH2382

---

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	42
Details	Repeat: {"description":"Kelch 2"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	49
Details	Repeat: {"description":"Kelch 3"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	54
Details	Repeat: {"description":"Kelch 4"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	52
Details	Repeat: {"description":"Kelch 5"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
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_FI8
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
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	TYR272	activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
A	PHE290	activator, radical stabiliser
A	TYR495	activator, metal ligand, proton acceptor, proton donor
A	HIS496	metal ligand
A	HIS581	metal ligand

---