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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PJX

0.85 ANGSTROM STRUCTURE OF SQUID GANGLION DFPASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0008150	biological_process	biological_process
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0047862	molecular_function	diisopropyl-fluorophosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 491

Chain	Residue
A	GLU21
A	ASN120
A	ASN175
A	ASP229
A	HOH502
A	HOH524
A	HOH604

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 492

Chain	Residue
A	HIS274
A	HOH509
A	HOH615
A	HOH623
A	ASP232
A	LEU273

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ME2 A 471

Chain	Residue
A	VAL5
A	GLU7
A	HIS248
A	ARG264
A	MES411
A	HOH976
A	HOH1047

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE MES A 411

Chain	Residue
A	GLU7
A	LYS43
A	PRO44
A	ASN67
A	GLY68
A	TYR69
A	ARG91
A	ARG264
A	PHE311
A	ME2471
A	HOH508
A	HOH628
A	HOH728
A	HOH1127
A	HOH1128

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MES A 412

Chain	Residue
A	GLU65
A	VAL66
A	THR102
A	PHE103
A	GLN258
A	HOH598
A	HOH687
A	HOH1129

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 421

Chain	Residue
A	LYS57
A	VAL167
A	ASP168
A	ILE211
A	MXE451
A	HOH859

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EDO A 422

Chain	Residue
A	PHE86
A	PHE124
A	PHE158
A	THR159
A	THR160
A	PEG461
A	HOH517
A	HOH692
A	HOH702
A	HOH858
A	HOH979

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 423

Chain	Residue
A	ARG115
A	GLU138
A	ASN289
A	TRP293
A	HOH516
A	HOH617
A	HOH959

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 424

Chain	Residue
A	PRO196
A	LYS198
A	THR223
A	HIS224
A	PGE433
A	HOH647
A	HOH970

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 425

Chain	Residue
A	HIS219
A	ILE220
A	PRO221
A	GLN258
A	HOH876

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 426

Chain	Residue
A	MET148
A	ASP184
A	GLU225
A	PHE314
A	PGE433
A	HOH581
A	HOH890
A	HOH906
A	HOH1001

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 427

Chain	Residue
A	GLY256
A	GLY257
A	GLN258
A	LYS260
A	PEG462
A	HOH877
A	HOH1123

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 428

Chain	Residue
A	HOH1082
A	HOH1125
A	HOH1126

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PGE A 433

Chain	Residue
A	GLN172
A	ASP184
A	PRO196
A	THR197
A	EDO424
A	EDO426
A	HOH644
A	HOH826
A	HOH970
A	HOH1102
A	HOH1103
A	MET148

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PGE A 434

Chain	Residue
A	ILE106
A	PHE158
A	GLY162
A	GLN163
A	MET164
A	THR279
A	LYS280
A	THR281
A	GLU296
A	HOH521
A	HOH544
A	HOH685
A	HOH735

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DXE A 441

Chain	Residue
A	ARG50
A	THR59
A	LYS151
A	TRP201
A	LYS214
A	MXE451
A	MXE452
A	HOH694
A	HOH768
A	HOH824
A	HOH977

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DXE A 442

Chain	Residue
A	TRP244
A	LYS269
A	HIS287
A	GOL401
A	HOH734

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DXE A 443

Chain	Residue
A	PRO8
A	LYS280
A	GLU296
A	TRP297
A	PEG461
A	HOH532
A	HOH770
A	HOH893
A	HOH954

site_id	CC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MXE A 451

Chain	Residue
A	LYS58
A	THR59
A	ASN213
A	LYS214
A	EDO421
A	DXE441
A	HOH569
A	HOH768
A	HOH859
A	HOH923

site_id	CC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MXE A 452

Chain	Residue
A	LYS151
A	THR169
A	ALA170
A	PHE171
A	GLU194
A	LYS214
A	DXE441
A	HOH531
A	HOH670
A	HOH694

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 401

Chain	Residue
A	GLU37
A	GLY312
A	ILE313
A	PHE314
A	DXE442
A	HOH619

site_id	CC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 403

Chain	Residue
A	PRO8
A	LEU9
A	PHE10
A	ASP143
A	LYS310
A	HOH559
A	HOH716
A	HOH728

site_id	CC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG A 461

Chain	Residue
A	GLN84
A	ILE106
A	LYS280
A	EDO422
A	DXE443
A	HOH639
A	HOH702
A	HOH832
A	HOH858

site_id	CC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG A 462

Chain	Residue
A	LYS63
A	GLU65
A	ASP255
A	GLY256
A	GLY257
A	EDO427
A	HOH573
A	HOH629
A	HOH844

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:15966726

Chain	Residue	Details
A	HIS287

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	GLU21
A	ASN120
A	ASN175
A	ASP229

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:11435114, ECO:0000269\|PubMed:14501113

Chain	Residue	Details
A	ASP232
A	LEU273
A	HIS274

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1e1a

Chain	Residue	Details
A	HIS287
A	GLU37

site_id	MCSA1
Number of Residues	6
Details	M-CSA 686

Chain	Residue	Details
A	GLU21	increase nucleophilicity, metal ligand, proton acceptor
A	GLU37	electrostatic stabiliser, increase basicity
A	ASN120	metal ligand
A	ASN175	metal ligand
A	ASP229	covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor
A	HIS287	increase nucleophilicity, proton acceptor

226707

PDB entries from 2024-10-30

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