Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XC1

Full-length Tailspike Protein Mutant Y108W of Bacteriophage P22

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0019058	biological_process	viral life cycle
A	0019062	biological_process	virion attachment to host cell
A	0044409	biological_process	symbiont entry into host
A	0046718	biological_process	symbiont entry into host cell
A	0051701	biological_process	biological process involved in interaction with host
A	0052775	molecular_function	endo-1,3-alpha-L-rhamnosidase activity
A	0098015	cellular_component	virus tail
A	0098024	cellular_component	virus tail, fiber
A	0098671	biological_process	adhesion receptor-mediated virion attachment to host cell
A	0098994	biological_process	symbiont entry into host cell via disruption of host cell envelope
A	0098995	biological_process	symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0019058	biological_process	viral life cycle
B	0019062	biological_process	virion attachment to host cell
B	0044409	biological_process	symbiont entry into host
B	0046718	biological_process	symbiont entry into host cell
B	0051701	biological_process	biological process involved in interaction with host
B	0052775	molecular_function	endo-1,3-alpha-L-rhamnosidase activity
B	0098015	cellular_component	virus tail
B	0098024	cellular_component	virus tail, fiber
B	0098671	biological_process	adhesion receptor-mediated virion attachment to host cell
B	0098994	biological_process	symbiont entry into host cell via disruption of host cell envelope
B	0098995	biological_process	symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0019058	biological_process	viral life cycle
C	0019062	biological_process	virion attachment to host cell
C	0044409	biological_process	symbiont entry into host
C	0046718	biological_process	symbiont entry into host cell
C	0051701	biological_process	biological process involved in interaction with host
C	0052775	molecular_function	endo-1,3-alpha-L-rhamnosidase activity
C	0098015	cellular_component	virus tail
C	0098024	cellular_component	virus tail, fiber
C	0098671	biological_process	adhesion receptor-mediated virion attachment to host cell
C	0098994	biological_process	symbiont entry into host cell via disruption of host cell envelope
C	0098995	biological_process	symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1667

Chain	Residue
A	SER568
A	LYS569
A	THR570
A	LEU571
C	TYR74
C	ASN75
C	HOH2084
C	HOH2086

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1668

Chain	Residue
A	GLU469
A	GLY494
A	ALA495
A	HOH2771
A	HIS468

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1669

Chain	Residue
A	HIS420
A	LEU466
A	HIS468
A	SER493
A	HOH2551

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1670

Chain	Residue
A	LEU663
A	HOH2762
B	LEU663
B	HOH2736
C	LEU663
C	HOH2728

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PE4 A 1671

Chain	Residue
A	ASN340
A	ASN378
A	ASP411
A	TYR412

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PE4 A 1672

Chain	Residue
A	GLN98
A	VAL99
A	ASP100
A	TYR101
B	ARG13
B	LEU78
B	HOH2129

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 1667

Chain	Residue
B	LEU406
B	ASP407
B	ARG408
B	PRO413
B	ILE414
B	THR415
B	HOH2247
B	HOH2531
B	HOH2540

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1668

Chain	Residue
A	LYS186
B	LYS170
B	ALA171
B	PHE194
B	HOH2742
B	HOH2743

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1669

Chain	Residue
B	ASN425
B	HOH2744
B	HOH2745
C	ASP210
C	GLN212

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 1670

Chain	Residue
B	LEU466
B	HIS468
B	SER493
B	HOH2569
B	HOH2746
B	HOH2747
B	HOH2748

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PE4 B 1671

Chain	Residue
B	ASN340
B	ASN378
B	ASP411
B	TYR412

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 1672

Chain	Residue
A	ARG20
A	SER97
A	HOH2151
B	LYS228
B	HOH2319
B	HOH2750

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1667

Chain	Residue
C	ASP407
C	ARG408
C	PRO413
C	ILE414
C	THR415
C	HOH2733
C	HOH2734

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1668

Chain	Residue
C	TYR417
C	LYS446
C	LYS653
C	ASN655
C	GLU657
C	HOH2505
C	HOH2735

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1669

Chain	Residue
C	THR235
C	VAL236
C	LYS302
C	HOH2736
C	HOH2737
C	HOH2738

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1670

Chain	Residue
C	PRO131
C	ARG148
C	TYR150
C	ASN151
C	HOH2739
C	HOH2740

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 1671

Chain	Residue
C	HOH2741
C	SER557

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1672

Chain	Residue
C	THR307
C	GLU309
C	LEU337
C	TRP365
C	HOH2742

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PE4 C 1673

Chain	Residue
C	ASN340
C	ASN378
C	ASP411
C	TYR412
C	HOH2743

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:8889178

Chain	Residue	Details
A	GLU359
A	ASP392
A	ASP395
B	GLU359
B	ASP392
B	ASP395
C	GLU359
C	ASP392
C	ASP395

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