1FDI

OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI COMPLEXED WITH THE INHIBITOR NITRITE

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	0043546	molecular_function	molybdopterin cofactor binding
A	0045271	cellular_component	respiratory chain complex I
A	0045333	biological_process	cellular respiration
A	0046872	molecular_function	metal ion binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	1990204	cellular_component	oxidoreductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO2 A 804

Chain	Residue
A	SEC140
A	HIS141
A	ARG333
A	GLY334
A	GLN335
A	VAL338
A	6MO803

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 A 800

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

---

site_id	AC3
Number of Residues	32
Details	BINDING SITE FOR RESIDUE MGD A 801

Chain	Residue
A	ARG110
A	GLY111
A	THR112
A	VAL139
A	SEC140
A	MET297
A	GLN301
A	GLN335
A	GLY402
A	GLU403
A	ASP404
A	THR408
A	GLN428
A	ASP429
A	ILE430
A	PHE431
A	THR433
A	SER445
A	THR446
A	HIS451
A	ASP478
A	THR579
A	ARG581
A	SER587
A	CYS588
A	TYR654
A	CYS661
A	ASN662
A	TYR678
A	MGD802
A	6MO803
A	HOH829

---

site_id	AC4
Number of Residues	34
Details	BINDING SITE FOR RESIDUE MGD A 802

Chain	Residue
A	LYS44
A	SEC140
A	PHE173
A	GLY174
A	TYR175
A	ASN176
A	ASP179
A	SER180
A	CYS201
A	ASP202
A	PRO203
A	ARG204
A	LEU218
A	GLY221
A	ASN223
A	GLY296
A	MET297
A	GLY298
A	PHE302
A	GLY334
A	GLN335
A	SER578
A	VAL580
A	ARG581
A	GLU582
A	VAL583
A	HIS585
A	TYR586
A	SER587
A	LYS679
A	MGD801
A	6MO803
A	HOH805
A	HOH832

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 6MO A 803

Chain	Residue
A	SEC140
A	MGD801
A	MGD802
A	NO2804

---

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	CYS42
A	SF4800
A	CYS8
A	CYS11
A	CYS15

---

site_id	MO4
Number of Residues	5
Details	THE MOLYBDENUM ATOM IS COORDINATED TO THE SELENIUM ATOM OF SEC 140, THE O1 OXYGEN ATOM OF NITRITE 804 AND THE FOUR SULFUR ATOMS OF MGD 801 AND MGD 802.

Chain	Residue
A	SEC140
A	MGD801
A	MGD802
A	6MO803
A	NO2804

---

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	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01004, ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855

Chain	Residue	Details
A	CYS8
A	TYR10
A	CYS11
A	CYS15
A	CYS42

---

site_id	SWS_FT_FI4
Number of Residues	11
Details	BINDING: BINDING => ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855

Chain	Residue	Details
A	LYS44
A	TYR678
A	LYS679
A	MET297
A	GLN301
A	GLN335
A	SER445
A	ASP478
A	CYS588
A	TYR654
A	GLN655

---

site_id	SWS_FT_FI5
Number of Residues	10
Details	BINDING:

Chain	Residue	Details
A	ARG110
A	CYS661
A	SEC140
A	PHE173
A	CYS201
A	GLY221
A	GLY402
A	GLN428
A	THR579
A	ARG581

---

site_id	SWS_FT_FI6
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	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
A	ASN132

---

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

---