5YHA

Crystal structure of Pd(allyl)/Wild Type Polyhedra

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue CL A 301

Chain	Residue
A	ALA2
A	LEU31

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site_id	AC2
Number of Residues	3
Details	binding site for residue PLL A 302

Chain	Residue
A	ARG209
A	CYS211
A	PLL303

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site_id	AC3
Number of Residues	4
Details	binding site for residue PLL A 303

Chain	Residue
A	GLU63
A	CYS211
A	PLL302
A	PD306

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site_id	AC4
Number of Residues	7
Details	binding site for residue PLL A 304

Chain	Residue
A	HIS141
A	TRP143
A	GLU144
A	ARG155
A	HIS238
A	SER239
A	HOH411

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site_id	AC5
Number of Residues	2
Details	binding site for residue PD A 305

Chain	Residue
A	HIS76
A	HIS76

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site_id	AC6
Number of Residues	3
Details	binding site for residue PD A 306

Chain	Residue
A	LYS66
A	CYS211
A	PLL303

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site_id	AC7
Number of Residues	1
Details	binding site for residue PD A 307

Chain	Residue
A	HIS170

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site_id	AC8
Number of Residues	4
Details	binding site for residue PD A 308

Chain	Residue
A	LYS58
A	CYS204
A	CYS204
A	HOH509

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site_id	AC9
Number of Residues	1
Details	binding site for residue PD A 309

Chain	Residue
A	HIS238

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site_id	AD1
Number of Residues	6
Details	binding site for residue EDO A 310

Chain	Residue
A	ASP3
A	GLY46
A	PHE100
A	ALA216
A	GLU217
A	HOH421

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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