2VKD

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF LETHAL TOXIN FROM CLOSTRIDIUM SORDELLII IN COMPLEX WITH UDP-GLC AND MANGANESE ION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016757	molecular_function	glycosyltransferase activity
B	0016757	molecular_function	glycosyltransferase activity
C	0016757	molecular_function	glycosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A1543

Chain	Residue
A	ASP288
A	GLU515
A	UPG1544
A	HOH2046
A	HOH2047

---

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE UPG A1544

Chain	Residue
A	LEU265
A	SER269
A	ASP270
A	ARG273
A	TYR284
A	ASP286
A	VAL287
A	ASP288
A	ASN384
A	GLN385
A	THR465
A	GLU515
A	SER518
A	LEU519
A	TRP520
A	MN1543
A	HOH2046
A	HOH2047
A	ILE101
A	TRP102
A	ILE103
A	ASN139

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN A1551

Chain	Residue
A	ASP280
B	GLU219

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN A1552

Chain	Residue
A	GLU219
C	ASP280

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN B1541

Chain	Residue
B	ASP288
B	GLU515
B	UPG1544

---

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE UPG B1544

Chain	Residue
B	ILE101
B	TRP102
B	ILE103
B	ASN139
B	LEU265
B	SER269
B	ASP270
B	ARG273
B	TYR284
B	ASP286
B	VAL287
B	ASP288
B	ASN384
B	GLN385
B	THR465
B	GLU515
B	SER518
B	LEU519
B	TRP520
B	MN1541
B	HOH2057

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C1542

Chain	Residue
C	ASP288
C	GLU515
C	UPG1544
C	HOH2044

---

site_id	AC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE UPG C1544

Chain	Residue
C	ILE101
C	TRP102
C	ILE103
C	ASN139
C	LEU265
C	ALA266
C	SER269
C	ASP270
C	ARG273
C	TYR284
C	ASP286
C	VAL287
C	ASP288
C	ASN384
C	GLN385
C	THR465
C	GLU515
C	SER518
C	LEU519
C	TRP520
C	MN1542
C	HOH2044

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:18325534, ECO:0000269|PubMed:18505687, ECO:0007744|PDB:2VKD, ECO:0007744|PDB:2VKH, ECO:0007744|PDB:2VL8

Chain	Residue	Details
A	ILE101
C	ASN139
C	LEU265
C	ASP286
A	ASN139
A	LEU265
A	ASP286
B	ILE101
B	ASN139
B	LEU265
B	ASP286
C	ILE101

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:18325534, ECO:0007744|PDB:2VKD, ECO:0007744|PDB:2VKH

Chain	Residue	Details
A	ASP288
A	GLU515
B	ASP288
B	GLU515
C	ASP288
C	GLU515

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:18325534, ECO:0000269|PubMed:18505687, ECO:0007744|PDB:2VKH, ECO:0007744|PDB:2VL8

Chain	Residue	Details
A	SER518
B	SER518
C	SER518

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P16154

Chain	Residue	Details
A	GLU545
B	GLU545
C	GLU545

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P18177

Chain	Residue	Details
A	ASP546
B	ASP546
C	ASP546

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P18177

Chain	Residue	Details
A	LEU543
B	LEU543
C	LEU543

---