Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2DDB

Crystal structure of pseudecin from Pseudechis porphyriacus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0035821	biological_process	modulation of process of another organism
A	0046872	molecular_function	metal ion binding
A	0090729	molecular_function	toxin activity
A	0099106	molecular_function	ion channel regulator activity
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0035821	biological_process	modulation of process of another organism
B	0046872	molecular_function	metal ion binding
B	0090729	molecular_function	toxin activity
B	0099106	molecular_function	ion channel regulator activity
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0035821	biological_process	modulation of process of another organism
C	0046872	molecular_function	metal ion binding
C	0090729	molecular_function	toxin activity
C	0099106	molecular_function	ion channel regulator activity
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0035821	biological_process	modulation of process of another organism
D	0046872	molecular_function	metal ion binding
D	0090729	molecular_function	toxin activity
D	0099106	molecular_function	ion channel regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 301

Chain	Residue
A	SER72
A	GLN73
A	SER127
A	HOH774
A	HOH977
B	HOH976

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 302

Chain	Residue
C	GOL326
C	HOH1000
C	SER72
C	GLN73
C	SER127

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 303

Chain	Residue
A	HOH568
B	SER72
B	GLN73
B	SER127
B	HOH957

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 304

Chain	Residue
D	SER72
D	GLN73
D	SER127
D	GOL327
D	HOH941

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 305

Chain	Residue
A	SER102
A	VAL103
A	ILE104
A	GLY105
D	SER183
D	LYS186

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 306

Chain	Residue
A	VAL20
A	LYS21
A	TYR85
A	ILE88
A	TYR107

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT B 307

Chain	Residue
B	VAL103
B	ILE104
B	GLY105
B	HOH1008
C	SER183
C	LYS186

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT B 308

Chain	Residue
A	LYS61
B	VAL20
B	LYS21
B	TYR85
B	ILE88
B	TYR107
B	HOH946

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT C 309

Chain	Residue
B	SER183
B	LYS186
C	SER102
C	VAL103
C	ILE104
C	GLY105

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT C 310

Chain	Residue
C	VAL20
C	LYS21
C	TYR85
C	ILE88
C	TYR107
C	HOH693

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT D 311

Chain	Residue
A	SER183
A	LYS186
D	VAL103
D	ILE104
D	GLY105
D	HOH800

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT D 312

Chain	Residue
D	VAL20
D	LYS21
D	TYR85
D	ILE88
D	TYR107
D	HOH958
D	HOH1055

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT C 313

Chain	Residue
C	LYS12
C	LEU16

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 314

Chain	Residue
A	GLU8
A	ARG46
A	HOH842
A	HOH1065
A	HOH1066

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A 315

Chain	Residue
A	TYR5
A	TRP77
A	ALA121
A	SER122
A	FMT324
A	HOH850

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 316

Chain	Residue
A	LYS124
A	SER127
B	SER102
B	VAL103
B	HOH915

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT A 317

Chain	Residue
A	SER126
A	ASN165
A	HOH805

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT C 318

Chain	Residue
C	ASN33

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT C 319

Chain	Residue
C	ASN173
C	LYS208
C	HOH751

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT D 320

Chain	Residue
A	HIS51
D	SER188
D	THR192

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT C 321

Chain	Residue
C	SER127
C	GOL326
D	SER102
D	VAL103
C	LYS124

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT D 322

Chain	Residue
C	SER102
C	VAL103
D	LYS124
D	SER127
D	GOL327
D	HOH945
D	HOH959

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT C 323

Chain	Residue
C	LYS182
C	SER202

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 324

Chain	Residue
A	SER122
A	FMT315
A	GOL331
A	HOH793

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT C 325

Chain	Residue
C	ASP11
C	ALA15
C	ARG18
C	HOH453
C	HOH863

site_id	CC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL C 326

Chain	Residue
C	SER72
C	GLN73
C	PRO74
C	SER127
C	TYR130
C	NA302
C	FMT321
C	HOH501
C	HOH791
D	GLU87
D	VAL103

site_id	CC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL D 327

Chain	Residue
C	GLU87
C	VAL103
D	SER72
D	GLN73
D	PRO74
D	SER127
D	TYR130
D	NA304
D	FMT322
D	HOH771
D	HOH959

site_id	DC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 328

Chain	Residue
A	ASN26
A	LYS151
A	HIS206
A	LYS208
A	ILE209
A	ILE210
A	HOH480
A	HOH932
A	HOH984

site_id	DC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 329

Chain	Residue
D	TYR5
D	TRP77
D	ALA121
D	SER122

site_id	DC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 330

Chain	Residue
A	LYS12
A	ALA15
A	LEU16
A	SER19
A	LYS41
A	ARG42
A	ASP45
A	HOH442
A	HOH761

site_id	DC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 331

Chain	Residue
A	ARG18
A	SER19
A	LYS21
A	ASP45
A	ALA123
A	LYS124
A	ARG166
A	FMT324

Functional Information from PROSITE/UniProt

site_id	PS01009
Number of Residues	11
Details	CRISP_1 CRISP family signature 1. GHYTQVVWykS

Chain	Residue	Details
A	GLY105-SER115

site_id	PS01010
Number of Residues	12
Details	CRISP_2 CRISP family signature 2. LYvCQYcPaGNI

Chain	Residue	Details
A	LEU131-ILE142

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:18931410

Chain	Residue	Details
A	THR23
A	SER78
B	THR23
B	SER78
C	THR23
C	SER78
D	THR23
D	SER78

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)