5TXU

1.95 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (SpoIID) from Clostridium difficile in Apo Conformation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0030435	biological_process	sporulation resulting in formation of a cellular spore
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 401

Chain	Residue
A	HIS134
A	CYS140
A	HIS145
A	CYS146

---

site_id	AC2
Number of Residues	5
Details	binding site for residue NA A 402

Chain	Residue
A	LYS179
A	LYS261
A	ASP352
A	TYR354
A	HOH623

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NA A 403

Chain	Residue
A	LYS294
A	HOH532
A	HOH634
A	HOH747
A	HOH749
A	HOH760

---

site_id	AC4
Number of Residues	4
Details	binding site for residue CL A 404

Chain	Residue
A	GLU101
A	PHE106
A	GLN324
A	HOH519

---

site_id	AC5
Number of Residues	3
Details	binding site for residue FMT A 405

Chain	Residue
A	TYR249
A	LYS282
A	HOH514

---

site_id	AC6
Number of Residues	5
Details	binding site for residue FMT A 406

Chain	Residue
A	GLU206
A	GLU207
A	VAL208
A	PHE209
A	HOH561

---

site_id	AC7
Number of Residues	6
Details	binding site for residue FMT A 407

Chain	Residue
A	MET90
A	ARG119
A	VAL175
A	GLY180
A	TYR354
A	HOH560

---

site_id	AC8
Number of Residues	1
Details	binding site for residue FMT A 408

Chain	Residue
A	TYR249

---

site_id	AC9
Number of Residues	4
Details	binding site for residue FMT A 409

Chain	Residue
A	TYR249
A	SER250
A	THR251
A	LYS282

---

site_id	AD1
Number of Residues	2
Details	binding site for residue FMT A 410

Chain	Residue
A	TYR185
A	ASN186

---

site_id	AD2
Number of Residues	3
Details	binding site for residue FMT A 411

Chain	Residue
A	SER103
A	GLU105
A	PHE106

---

site_id	AD3
Number of Residues	3
Details	binding site for residue FMT A 412

Chain	Residue
A	SER196
A	HOH519
A	HOH583

---

site_id	AD4
Number of Residues	3
Details	binding site for residue FMT A 413

Chain	Residue
A	LYS201
A	SER218
A	GLU220

---

site_id	AD5
Number of Residues	1
Details	binding site for residue FMT A 414

Chain	Residue
A	ILE81

---

site_id	AD6
Number of Residues	1
Details	binding site for residue FMT A 415

Chain	Residue
A	SER210

---

site_id	AD7
Number of Residues	4
Details	binding site for residue FMT A 416

Chain	Residue
A	ALA99
A	GLY100
A	GLU101
A	FMT420

---

site_id	AD8
Number of Residues	2
Details	binding site for residue FMT A 417

Chain	Residue
A	HOH568
A	HOH607

---

site_id	AD9
Number of Residues	2
Details	binding site for residue FMT A 418

Chain	Residue
A	HOH601
A	HOH609

---

site_id	AE1
Number of Residues	7
Details	binding site for residue FMT A 419

Chain	Residue
A	LYS229
A	LYS229
A	ASN296
A	TYR316
A	HOH503
A	HOH511
A	HOH583

---

site_id	AE2
Number of Residues	5
Details	binding site for residue FMT A 420

Chain	Residue
A	GLY100
A	GLU101
A	FMT416
A	HOH521
A	HOH558

---

site_id	AE3
Number of Residues	6
Details	binding site for residue DMS A 421

Chain	Residue
A	PRO222
A	TYR223
A	TYR335
A	HIS343
A	HOH539
A	HOH586

---

site_id	AE4
Number of Residues	8
Details	binding site for residue DMS A 422

Chain	Residue
A	THR197
A	THR273
A	ASN299
A	LYS314
A	GLY317
A	HIS318
A	GLY319
A	HOH604

---

site_id	AE5
Number of Residues	4
Details	binding site for residue DMS A 423

Chain	Residue
A	SER260
A	PHE304
A	GLY305
A	HOH665

---

site_id	AE6
Number of Residues	3
Details	binding site for residue DMS A 424

Chain	Residue
A	LEU193
A	TYR194
A	HIS318

---

site_id	AE7
Number of Residues	1
Details	binding site for residue DMS A 425

Chain	Residue
A	GLU333

---