Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4HOH

RIBONUCLEASE T1 (THR93ALA MUTANT) COMPLEXED WITH 2'GMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001411	cellular_component	hyphal tip
A	0003723	molecular_function	RNA binding
A	0004519	molecular_function	endonuclease activity
A	0004521	molecular_function	RNA endonuclease activity
A	0004540	molecular_function	RNA nuclease activity
A	0008150	biological_process	biological_process
A	0016829	molecular_function	lyase activity
A	0030428	cellular_component	cell septum
A	0046589	molecular_function	ribonuclease T1 activity
B	0001411	cellular_component	hyphal tip
B	0003723	molecular_function	RNA binding
B	0004519	molecular_function	endonuclease activity
B	0004521	molecular_function	RNA endonuclease activity
B	0004540	molecular_function	RNA nuclease activity
B	0008150	biological_process	biological_process
B	0016829	molecular_function	lyase activity
B	0030428	cellular_component	cell septum
B	0046589	molecular_function	ribonuclease T1 activity
C	0001411	cellular_component	hyphal tip
C	0003723	molecular_function	RNA binding
C	0004519	molecular_function	endonuclease activity
C	0004521	molecular_function	RNA endonuclease activity
C	0004540	molecular_function	RNA nuclease activity
C	0008150	biological_process	biological_process
C	0016829	molecular_function	lyase activity
C	0030428	cellular_component	cell septum
C	0046589	molecular_function	ribonuclease T1 activity
D	0001411	cellular_component	hyphal tip
D	0003723	molecular_function	RNA binding
D	0004519	molecular_function	endonuclease activity
D	0004521	molecular_function	RNA endonuclease activity
D	0004540	molecular_function	RNA nuclease activity
D	0008150	biological_process	biological_process
D	0016829	molecular_function	lyase activity
D	0030428	cellular_component	cell septum
D	0046589	molecular_function	ribonuclease T1 activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 105

Chain	Residue
C	GLY47
C	ASP49
C	HOH1218
C	HOH1219
D	TYR45

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA D 106

Chain	Residue
C	TYR45
D	GLY47
D	ASP49

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 2GP A 107

Chain	Residue
A	TYR38
A	HIS40
A	LYS41
A	TYR42
A	ASN43
A	ASN44
A	TYR45
A	GLU46
A	GLU58
A	ASN98
A	PHE100
A	HOH1059
A	HOH1138
D	HOH1072

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 2GP B 108

Chain	Residue
B	ASN36
B	TYR38
B	TYR42
B	ASN43
B	ASN44
B	TYR45
B	GLU46
B	GLU58
B	ASN98
B	PHE100
B	HOH1209

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 2GP C 109

Chain	Residue
A	SER53
A	HOH1020
C	HIS40
C	TYR42
C	ASN43
C	ASN44
C	TYR45
C	GLU46
C	PHE100
C	HOH1004
C	HOH1212

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE 2GP C 110

Chain	Residue
C	GLY74
C	ARG77
C	HIS92
C	ASN98
C	PHE100
C	HOH1004
C	HOH1212
C	HOH1215
C	HOH1217
A	SER53
A	SER54
A	PRO55
A	ASN81
A	GLU82
A	ASN83
A	HOH1020
A	HOH1201
C	ASN36
C	TYR38
C	HIS40
C	GLU58
C	PRO73

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 2GP D 111

Chain	Residue
D	TYR38
D	HIS40
D	LYS41
D	TYR42
D	ASN43
D	ASN44
D	TYR45
D	GLU46
D	GLU58
D	ASN98
D	PHE100
D	HOH1110
D	HOH1191

site_id	BI1
Number of Residues	5
Details	BINDING SITE.

Chain	Residue
A	TYR42
A	ASN43
A	ASN44
A	TYR45
A	GLU46

site_id	BI2
Number of Residues	5
Details	BINDING SITE.

Chain	Residue
B	TYR42
B	ASN43
B	ASN44
B	TYR45
B	GLU46

site_id	BI3
Number of Residues	5
Details	BINDING SITE.

Chain	Residue
C	TYR42
C	ASN43
C	ASN44
C	TYR45
C	GLU46

site_id	BI4
Number of Residues	5
Details	BINDING SITE.

Chain	Residue
D	TYR42
D	ASN43
D	ASN44
D	TYR45
D	GLU46

site_id	CA1
Number of Residues	1
Details	SITE.

Chain	Residue
C	ASP49

site_id	CA2
Number of Residues	1
Details	SITE.

Chain	Residue
D	ASP49

site_id	CT1
Number of Residues	5
Details	ACTIVE SITE.

Chain	Residue
A	TYR38
A	HIS40
A	GLU58
A	ARG77
A	HIS92

site_id	CT2
Number of Residues	5
Details	ACTIVE SITE.

Chain	Residue
B	HIS92
B	TYR38
B	HIS40
B	GLU58
B	ARG77

site_id	CT3
Number of Residues	5
Details	ACTIVE SITE.

Chain	Residue
C	TYR38
C	HIS40
C	GLU58
C	ARG77
C	HIS92

site_id	CT4
Number of Residues	5
Details	ACTIVE SITE.

Chain	Residue
D	TYR38
D	HIS40
D	GLU58
D	ARG77
D	HIS92

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:2844811

Chain	Residue	Details
A	HIS40
B	HIS40
C	HIS40
D	HIS40

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:2844811

Chain	Residue	Details
A	GLU58
B	GLU58
C	GLU58
D	GLU58

site_id	SWS_FT_FI3
Number of Residues	4
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	HIS92
B	HIS92
C	HIS92
D	HIS92

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1b2m

Chain	Residue	Details
A	GLU58
A	HIS40
A	HIS92

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1b2m

Chain	Residue	Details
B	GLU58
B	HIS40
B	HIS92

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1b2m

Chain	Residue	Details
C	GLU58
C	HIS40
C	HIS92

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1b2m

Chain	Residue	Details
D	GLU58
D	HIS40
D	HIS92

site_id	MCSA1
Number of Residues	6
Details	M-CSA 414

Chain	Residue	Details
A	TYR38	electrostatic stabiliser
A	HIS40	proton shuttle (general acid/base)
A	GLU58	proton shuttle (general acid/base)
A	ARG77	electrostatic stabiliser
A	HIS92	proton shuttle (general acid/base)
A	PHE100	electrostatic stabiliser

site_id	MCSA2
Number of Residues	6
Details	M-CSA 414

Chain	Residue	Details
B	TYR38	electrostatic stabiliser
B	HIS40	proton shuttle (general acid/base)
B	GLU58	proton shuttle (general acid/base)
B	ARG77	electrostatic stabiliser
B	HIS92	proton shuttle (general acid/base)
B	PHE100	electrostatic stabiliser

site_id	MCSA3
Number of Residues	6
Details	M-CSA 414

Chain	Residue	Details
C	TYR38	electrostatic stabiliser
C	HIS40	proton shuttle (general acid/base)
C	GLU58	proton shuttle (general acid/base)
C	ARG77	electrostatic stabiliser
C	HIS92	proton shuttle (general acid/base)
C	PHE100	electrostatic stabiliser

site_id	MCSA4
Number of Residues	6
Details	M-CSA 414

Chain	Residue	Details
D	TYR38	electrostatic stabiliser
D	HIS40	proton shuttle (general acid/base)
D	GLU58	proton shuttle (general acid/base)
D	ARG77	electrostatic stabiliser
D	HIS92	proton shuttle (general acid/base)
D	PHE100	electrostatic stabiliser

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