5FEX

HydE from T. maritima in complex with Se-adenosyl-L-selenocysteine (tfinal of the reaction)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016491	molecular_function	oxidoreductase activity
A	0016740	molecular_function	transferase activity
A	0042364	biological_process	water-soluble vitamin biosynthetic process
A	0044272	biological_process	sulfur compound biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue SF4 A 401

Chain	Residue
A	CYS63
A	CYS67
A	CYS70
A	MET411

---

site_id	AC2
Number of Residues	16
Details	binding site for residue CPS A 402

Chain	Residue
A	ARG284
A	MET324
A	LEU330
A	CPS406
A	HOH535
A	HOH605
A	HOH612
A	HOH673
A	HOH686
A	HOH764
A	HOH941
A	GLN98
A	PHE99
A	GLY100
A	GLY277
A	GLU280

---

site_id	AC3
Number of Residues	14
Details	binding site for residue CPS A 403

Chain	Residue
A	LYS37
A	ASP40
A	LYS170
A	ARG284
A	SER297
A	LYS315
A	ASP316
A	THR317
A	HOH595
A	HOH599
A	HOH628
A	HOH684
A	HOH746
A	HOH892

---

site_id	AC4
Number of Residues	9
Details	binding site for residue CPS A 404

Chain	Residue
A	ARG29
A	GLU33
A	THR247
A	LEU250
A	CPS405
A	HOH516
A	HOH632
A	HOH701
A	HOH957

---

site_id	AC5
Number of Residues	12
Details	binding site for residue CPS A 405

Chain	Residue
A	ARG29
A	GLU314
A	LYS315
A	THR317
A	ALA318
A	CPS404
A	CPS406
A	HOH586
A	HOH621
A	HOH656
A	HOH661
A	HOH689

---

site_id	AC6
Number of Residues	14
Details	binding site for residue CPS A 406

Chain	Residue
A	LYS128
A	PRO321
A	MET324
A	LYS325
A	GLU328
A	CPS402
A	CPS405
A	HOH662
A	HOH781
A	HOH784
A	HOH797
A	HOH894
A	HOH937
A	HOH954

---

site_id	AC7
Number of Residues	3
Details	binding site for residue CL A 407

Chain	Residue
A	ARG54
A	THR134
A	ARG155

---

site_id	AC8
Number of Residues	3
Details	binding site for residue CL A 408

Chain	Residue
A	ARG159
A	SEC412
A	HOH818

---

site_id	AC9
Number of Residues	2
Details	binding site for residue CL A 409

Chain	Residue
A	TYR306
A	SEC412

---

site_id	AD1
Number of Residues	12
Details	binding site for residue 5AD A 410

Chain	Residue
A	TYR69
A	ARG159
A	GLU161
A	MET199
A	PRO229
A	ILE231
A	LEU305
A	TYR306
A	MET411
A	SEC412
A	HOH649
A	HOH698

---

site_id	AD2
Number of Residues	11
Details	binding site for residue MET A 411

Chain	Residue
A	HOH649
A	SER108
A	SER136
A	GLY138
A	ARG180
A	TYR303
A	LEU305
A	SF4401
A	5AD410
A	HOH569
A	HOH601

---

site_id	AD3
Number of Residues	13
Details	binding site for residue SEC A 412

Chain	Residue
A	GLN107
A	ARG159
A	THR268
A	THR269
A	ALA270
A	TYR306
A	CL408
A	CL409
A	5AD410
A	HOH529
A	HOH609
A	HOH697
A	HOH793

---

Functional Information from PROSITE/UniProt

site_id	PS00216
Number of Residues	18
Details	SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. VMKMIELLGRKpgrdwgG

Chain	Residue	Details
A	VAL323-GLY340

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PIRSR:PIRSR004762-1, ECO:0000269|PubMed:16137685, ECO:0000269|PubMed:18400755, ECO:0000269|PubMed:19706452, ECO:0007744|PDB:3CIW, ECO:0007744|PDB:3CIX, ECO:0007744|PDB:3IIX

Chain	Residue	Details
A	CYS63

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PIRSR:PIRSR004762-1, ECO:0000269|PubMed:16137685, ECO:0007744|PDB:3CIW, ECO:0007744|PDB:3CIX, ECO:0007744|PDB:3IIX

Chain	Residue	Details
A	CYS67
A	CYS70

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744|PDB:3CIX, ECO:0007744|PDB:3IIZ, ECO:0007744|PDB:4JXC, ECO:0007744|PDB:4JY8, ECO:0007744|PDB:4JY9, ECO:0007744|PDB:4JYE

Chain	Residue	Details
A	SER311

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:3CIX, ECO:0007744|PDB:4JY8, ECO:0007744|PDB:4JY9, ECO:0007744|PDB:4JYE

Chain	Residue	Details
A	SER319
A	SER322

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