1DIQ

CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004458	molecular_function	D-lactate dehydrogenase (cytochrome) activity
A	0008720	molecular_function	D-lactate dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0018695	molecular_function	4-cresol dehydrogenase (hydroxylating) activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0071949	molecular_function	FAD binding
A	1903457	biological_process	lactate catabolic process
B	0003824	molecular_function	catalytic activity
B	0004458	molecular_function	D-lactate dehydrogenase (cytochrome) activity
B	0008720	molecular_function	D-lactate dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0018695	molecular_function	4-cresol dehydrogenase (hydroxylating) activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0071949	molecular_function	FAD binding
B	1903457	biological_process	lactate catabolic process
C	0009055	molecular_function	electron transfer activity
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 701

Chain	Residue
B	MET48
B	GLY94
B	GLY96
B	SER97

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 702

Chain	Residue
A	MET48
A	GLY94
A	GLY96
A	SER97

---

site_id	AC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD A 599

Chain	Residue
A	THR86
A	SER88
A	THR89
A	GLY90
A	ARG91
A	ASN92
A	PHE93
A	SER153
A	ALA154
A	PRO155
A	ALA159
A	GLY160
A	GLY163
A	ASN164
A	MET166
A	GLY169
A	VAL170
A	TYR172
A	GLY229
A	ILE230
A	CYS231
A	GLU380
A	TYR384
A	TRP394
A	ARG474
A	ARG512
A	PCR798
A	HOH823
A	TRP85

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site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PCR A 798

Chain	Residue
A	TYR95
A	TYR172
A	TRP285
A	GLU380
A	TRP394
A	GLU427
A	ILE429
A	VAL438
A	TYR473
A	FAD599

---

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC C 699

Chain	Residue
A	LEU378
A	PHE381
A	HOH879
B	LYS419
C	HOH275
C	VAL614
C	CYS615
C	CYS618
C	HIS619
C	VAL625
C	PRO627
C	LEU629
C	ARG632
C	TYR638
C	ILE642
C	VAL643
C	PHE647
C	ARG648
C	MET650

---

site_id	AC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD B 599

Chain	Residue
B	TRP85
B	THR86
B	SER88
B	THR89
B	GLY90
B	ARG91
B	ASN92
B	PHE93
B	SER153
B	ALA154
B	PRO155
B	ALA159
B	GLY160
B	GLY163
B	ASN164
B	MET166
B	GLY169
B	VAL170
B	TYR172
B	GLY229
B	CYS231
B	GLU380
B	TYR384
B	TRP394
B	ARG474
B	ARG512
B	PCR799
B	HOH905
B	HOH923

---

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PCR B 799

Chain	Residue
B	TRP394
B	GLU427
B	ILE429
B	VAL438
B	TYR473
B	FAD599
B	HOH821
B	TYR95
B	TYR172
B	TRP285
B	GLU380

---

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEC D 699

Chain	Residue
A	LYS419
B	PHE381
D	HOH84
D	VAL614
D	CYS615
D	CYS618
D	HIS619
D	VAL625
D	PRO627
D	LEU629
D	ARG632
D	TYR638
D	ILE642
D	VAL643
D	PHE647
D	ARG648
D	MET650

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: covalent

Chain	Residue	Details
C	CYS615
C	CYS618
D	CYS615
D	CYS618

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: axial binding residue

Chain	Residue	Details
C	HIS619
C	MET650
D	HIS619
D	MET650

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1dii

Chain	Residue	Details
A	TYR473
A	TYR95
A	ARG474
A	GLU380
A	GLU427
A	HIS436

---

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1dii

Chain	Residue	Details
B	TYR473
B	TYR95
B	ARG474
B	GLU380
B	GLU427
B	HIS436

---

site_id	MCSA1
Number of Residues	2
Details	M-CSA 141

Chain	Residue	Details
C	ALA649	polar interaction, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay
A	ARG512	activator, hydrogen bond donor
C	MET650	metal ligand, polar interaction, single electron acceptor, single electron donor, single electron relay
A	GLU286	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	TYR367	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	GLU380	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR384	covalently attached, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay
A	HIS436	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	TYR473	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	ARG474	electrostatic stabiliser, hydrogen bond donor

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 141

Chain	Residue	Details
D	ALA649	polar interaction, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay
B	ARG512	activator, hydrogen bond donor
D	MET650	metal ligand, polar interaction, single electron acceptor, single electron donor, single electron relay
B	GLU286	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	TYR367	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	GLU380	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	TYR384	covalently attached, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay
B	HIS436	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	TYR473	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	ARG474	electrostatic stabiliser, hydrogen bond donor

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