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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4A66

Mutations in the neighbourhood of CotA-laccase trinuclear site: D116A 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	4
Details	BINDING SITE FOR RESIDUE CU A 1512

Chain	Residue
A	HIS419
A	CYS492
A	HIS497
A	MET502

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 1513

Chain	Residue
A	HIS107
A	HIS153
A	HIS493
A	PER1527

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 1514

Chain	Residue
A	HIS424
A	HIS491
A	CU1515
A	PER1527
A	HIS155

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CU A 1515

Chain	Residue
A	HIS105
A	HIS107
A	HIS422
A	HIS424
A	CU1514
A	PER1527
A	HOH2137

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1516

Chain	Residue
A	PHE292
A	SER293
A	TYR300
A	PRO457
A	HOH2310

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1517

Chain	Residue
A	LEU184
A	SER186
A	GLU348
A	HOH2219
A	HOH2267

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1518

Chain	Residue
A	ARG136
A	GLU137
A	VAL138
A	PRO247
A	HOH2173
A	HOH2266

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1519

Chain	Residue
A	ALA317
A	PRO328
A	ALA332
A	ASN333
A	HOH2289
A	HOH2447

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1520

Chain	Residue
A	GLU364
A	ARG429
A	TRP463
A	ALA478
A	THR480

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1521

Chain	Residue
A	ASP113
A	TYR118
A	TYR133
A	LYS135
A	ARG487
A	HOH2147

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1522

Chain	Residue
A	PRO284
A	ARG285
A	VAL287
A	TYR358
A	PRO458
A	LYS461

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1523

Chain	Residue
A	PHE81
A	PRO83
A	LEU206
A	PHE207
A	TYR208
A	HOH2117
A	HOH2239
A	HOH2246

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1524

Chain	Residue
A	GLU188
A	GLU244
A	TYR250
A	HOH2224

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1525

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

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1526

Chain	Residue
A	ASN75
A	LEU76
A	LYS125
A	GLN367
A	LYS402

site_id	BC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PER A 1527

Chain	Residue
A	HIS105
A	HIS107
A	HIS153
A	HIS155
A	HIS422
A	HIS424
A	HIS491
A	HIS493
A	CU1513
A	CU1514
A	CU1515
A	HOH2194

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	ALA116

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 2024-10-16

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