1AA6

REDUCED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003954	molecular_function	NADH dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006007	biological_process	glucose catabolic process
A	0008863	molecular_function	formate dehydrogenase (NAD+) activity
A	0009061	biological_process	anaerobic respiration
A	0009326	cellular_component	formate dehydrogenase complex
A	0015942	biological_process	formate metabolic process
A	0015944	biological_process	formate oxidation
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
A	0019628	biological_process	urate catabolic process
A	0019645	biological_process	anaerobic electron transport chain
A	0022904	biological_process	respiratory electron transport chain
A	0043546	molecular_function	molybdopterin cofactor binding
A	0045333	biological_process	cellular respiration
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	1990204	cellular_component	oxidoreductase complex

Functional Information from PDB Data

site_id	4MO
Number of Residues	4
Details	THE MOLYBDENUM ATOM IS COORDINATED TO THE SELENIUM ATOM OF SEC 140 AND THE FOUR SULFUR ATOMS OF MGD 801 AND MGD 802.

Chain	Residue
A	SEC140
A	MGD801
A	MGD802
A	4MO803

---

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 A 800

Chain	Residue
A	CYS8
A	TYR10
A	CYS11
A	SER13
A	CYS15
A	LEU41
A	CYS42
A	LYS44
A	PRO182
A	ILE183

---

site_id	AC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE MGD A 801

Chain	Residue
A	ARG110
A	GLY111
A	THR112
A	VAL139
A	SEC140
A	GLN335
A	GLY402
A	GLU403
A	ASP404
A	THR408
A	ASP409
A	ALA410
A	GLN428
A	ASP429
A	ILE430
A	THR433
A	SER445
A	THR446
A	ASP478
A	CYS588
A	TYR654
A	TYR678
A	MGD802
A	4MO803
A	HOH825
A	HOH830
A	HOH840
A	HOH848
A	HOH849
A	HOH853

---

site_id	AC3
Number of Residues	32
Details	BINDING SITE FOR RESIDUE MGD A 802

Chain	Residue
A	LYS44
A	PHE173
A	GLY174
A	TYR175
A	ASN176
A	ASP179
A	SER180
A	CYS201
A	ASP202
A	PRO203
A	ARG204
A	ILE206
A	GLY221
A	ASN223
A	GLY296
A	MET297
A	GLY298
A	PHE302
A	GLY334
A	VAL580
A	ARG581
A	GLU582
A	VAL583
A	HIS585
A	TYR586
A	SER587
A	GLN655
A	LYS679
A	MGD801
A	4MO803
A	HOH804
A	HOH833

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 4MO A 803

Chain	Residue
A	SEC140
A	MGD801
A	MGD802

---

site_id	FS4
Number of Residues	5
Details	THE IRON SULFUR CLUSTER IS COORDINATED TO THE SULFUR ATOMS OF CYS 8, CYS 11, CYS 15, AND CYS 42.

Chain	Residue
A	SF4800
A	CYS8
A	CYS11
A	CYS15
A	CYS42

---

Functional Information from PROSITE/UniProt

site_id	PS00490
Number of Residues	18
Details	MOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TkTAsaADVILPsTSwgE

Chain	Residue	Details
A	THR433-GLU450

---

site_id	PS00551
Number of Residues	18
Details	MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. TvCpy.CASgCkInLvvd.N

Chain	Residue	Details
A	THR6-ASN23

---

site_id	PS00932
Number of Residues	28
Details	MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AkrlGIeDeAlVwVhSrkGkiitrAqVS

Chain	Residue	Details
A	ALA615-SER642

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Electron donor/acceptor

Chain	Residue	Details
A	LYS44

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor

Chain	Residue	Details
A	SEC140

---

site_id	SWS_FT_FI3
Number of Residues	23
Details	BINDING: BINDING => ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855, ECO:0007744|PDB:1AA6, ECO:0007744|PDB:1FDI, ECO:0007744|PDB:1FDO, ECO:0007744|PDB:2IV2

Chain	Residue	Details
A	CYS8
A	CYS201
A	ASP202
A	ARG204
A	GLY221
A	ASN223
A	ASP404
A	GLN428
A	ASP429
A	ASP478
A	ARG581
A	CYS11
A	GLU582
A	HIS585
A	SER587
A	LYS679
A	CYS15
A	CYS42
A	ARG110
A	SEC140
A	ASN176
A	ASP179
A	SER180

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:9036855, ECO:0007744|PDB:1AA6, ECO:0007744|PDB:1FDI, ECO:0007744|PDB:1FDO

Chain	Residue	Details
A	MET297
A	SER445

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855, ECO:0007744|PDB:1AA6, ECO:0007744|PDB:1FDI, ECO:0007744|PDB:2IV2

Chain	Residue	Details
A	GLN335

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855, ECO:0007744|PDB:1FDI, ECO:0007744|PDB:1FDO, ECO:0007744|PDB:2IV2

Chain	Residue	Details
A	THR408
A	TYR678

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	SITE: Important for catalytic activity

Chain	Residue	Details
A	HIS141
A	ARG333

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9036855, 16830149

Chain	Residue	Details
A	LYS44
A	CSE140

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 562

Chain	Residue	Details
A	LYS44	electrostatic stabiliser
A	SEC140	electrophile, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
A	HIS141	electrostatic stabiliser, proton acceptor
A	ARG333	electrostatic stabiliser, hydrogen bond donor

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