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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WSD

Proximal mutations at the type 1 Cu site of CotA-laccase: I494A mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0030435	biological_process	sporulation resulting in formation of a cellular spore
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 601

Chain	Residue
A	HIS419
A	CYS492
A	HIS497
A	MET502
A	HOH2519

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 602

Chain	Residue
A	HIS107
A	HIS153
A	HIS493
A	OXY605

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 603

Chain	Residue
A	HIS155
A	HIS424
A	HIS491
A	CU604
A	OXY605

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CU A 604

Chain	Residue
A	HIS105
A	HIS107
A	HIS422
A	HIS424
A	CU603
A	OXY605
A	HOH2177

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OXY A 605

Chain	Residue
A	HIS105
A	HIS107
A	HIS153
A	HIS155
A	HIS422
A	HIS424
A	HIS491
A	HIS493
A	CU602
A	CU603
A	CU604

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 701

Chain	Residue
A	ASP113
A	TYR118
A	TYR133
A	LYS135
A	HOH2593

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 702

Chain	Residue
A	LYS25
A	TYR69
A	VAL138
A	THR307
A	ALA308
A	TYR309
A	GLU310
A	HOH2594

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 703

Chain	Residue
A	ASN74
A	LEU76
A	PRO77
A	VAL100
A	SER124
A	LYS125
A	HOH2595

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 704

Chain	Residue
A	GLU188
A	GLU244
A	TYR250
A	HOH2596

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 705

Chain	Residue
A	ARG136
A	GLU137
A	VAL138
A	PRO247
A	HOH2597
A	HOH2598

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 706

Chain	Residue
A	ASP268
A	ALA317
A	PRO328
A	ALA332
A	ASN333
A	HOH2599
A	HOH2600

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 707

Chain	Residue
A	LYS183
A	LEU184
A	SER186
A	GLU348
A	SER349
A	HOH2601

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 708

Chain	Residue
A	GLU61
A	ILE173
A	HIS175
A	ASP190
A	PRO192
A	HOH2106
A	HOH2298
A	HOH2602
A	HOH2603

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 709

Chain	Residue
A	ASN269
A	GLY271
A	ASP272
A	ASP305
A	TYR309
A	HOH2367

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 710

Chain	Residue
A	VAL426
A	SER427
A	THR480
A	GLY482
A	HOH2253
A	HOH2573
A	HOH2605
A	HOH2606
A	HOH2607

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 711

Chain	Residue
A	THR130
A	GLY131
A	PHE134
A	HOH2608
A	HOH2609

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 712

Chain	Residue
A	SER186
A	TYR189
A	ARG248
A	LYS346
A	GLU348
A	HOH2601

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: type 2 copper site => ECO:0000269\|PubMed:12637519, ECO:0000269\|PubMed:14764581, ECO:0000269\|PubMed:16234932, ECO:0000269\|PubMed:20822511, ECO:0007744\|PDB:1GSK, ECO:0007744\|PDB:1OF0, ECO:0007744\|PDB:1W6L, ECO:0007744\|PDB:1W6W, ECO:0007744\|PDB:1W8E, ECO:0007744\|PDB:2BHF, ECO:0007744\|PDB:2X87, ECO:0007744\|PDB:2X88, ECO:0007744\|PDB:3ZDW

Chain	Residue	Details
A	HIS105
A	HIS422

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: type 3 copper site => ECO:0000269\|PubMed:12637519, ECO:0000269\|PubMed:14764581, ECO:0000269\|PubMed:16234932, ECO:0000269\|PubMed:20822511, ECO:0000269\|PubMed:27050268, ECO:0007744\|PDB:1GSK, ECO:0007744\|PDB:1OF0, ECO:0007744\|PDB:1W6L, ECO:0007744\|PDB:1W6W, ECO:0007744\|PDB:1W8E, ECO:0007744\|PDB:2BHF, ECO:0007744\|PDB:2X87, ECO:0007744\|PDB:2X88, ECO:0007744\|PDB:3ZDW, ECO:0007744\|PDB:4YVN, ECO:0007744\|PDB:4YVU

Chain	Residue	Details
A	HIS107
A	HIS153
A	HIS155
A	HIS424
A	HIS491
A	HIS493

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: type 1 copper site => ECO:0000269\|PubMed:12637519, ECO:0000269\|PubMed:14764581, ECO:0000269\|PubMed:16234932, ECO:0000269\|PubMed:20822511, ECO:0000269\|PubMed:27050268, ECO:0007744\|PDB:1GSK, ECO:0007744\|PDB:1OF0, ECO:0007744\|PDB:1W6L, ECO:0007744\|PDB:1W6W, ECO:0007744\|PDB:1W8E, ECO:0007744\|PDB:2BHF, ECO:0007744\|PDB:2X87, ECO:0007744\|PDB:2X88, ECO:0007744\|PDB:3ZDW, ECO:0007744\|PDB:4YVN, ECO:0007744\|PDB:4YVU

Chain	Residue	Details
A	HIS419
A	CYS492
A	HIS497

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: type 1 copper site => ECO:0000269\|PubMed:12637519, ECO:0000269\|PubMed:16234932, ECO:0000269\|PubMed:20822511, ECO:0000269\|PubMed:27050268, ECO:0007744\|PDB:1GSK, ECO:0007744\|PDB:1OF0, ECO:0007744\|PDB:1W6L, ECO:0007744\|PDB:1W8E, ECO:0007744\|PDB:2BHF, ECO:0007744\|PDB:2X87, ECO:0007744\|PDB:2X88, ECO:0007744\|PDB:4YVN, ECO:0007744\|PDB:4YVU

Chain	Residue	Details
A	MET502

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Plays a crucial role in the protonation steps => ECO:0000305\|PubMed:22481612

Chain	Residue	Details
A	ASP116

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Plays a crucial role in the protonation steps => ECO:0000305\|PubMed:20200715, ECO:0000305\|PubMed:20822511, ECO:0000305\|PubMed:22481612

Chain	Residue	Details
A	GLU498

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PDB entries from 2025-06-11

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