1RU4

Crystal structure of pectate lyase Pel9A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016829	molecular_function	lyase activity
A	0016837	molecular_function	carbon-oxygen lyase activity, acting on polysaccharides
A	0030570	molecular_function	pectate lyase activity
A	0045490	biological_process	pectin catabolic process
A	0046872	molecular_function	metal ion binding
A	0052009	biological_process	symbiont-mediated disruption of host cell wall

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1

Chain	Residue
A	ASP209
A	ASP233
A	ASP234
A	ASP237
A	HOH459
A	HOH573

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 2

Chain	Residue
A	ASP418
A	GLU423
A	HOH482
A	ASN402
A	SER413
A	ALA416

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:14670977

Chain	Residue	Details
A	LYS273

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:14670977, ECO:0007744|PDB:1RU4

Chain	Residue	Details
A	ASP209
A	ASP233
A	ASP234
A	ASP237
A	ASN402
A	SER413
A	ALA416
A	ASP418
A	GLU423

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 14670977

Chain	Residue	Details
A	LYS273
A	ASN268

---

site_id	MCSA1
Number of Residues	2
Details	M-CSA 184

Chain	Residue	Details
A	ASN268	electrostatic stabiliser, hydrogen bond donor, increase acidity
A	LYS273	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---