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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JZS

Structure of the Manganese Protoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan in complex with Pyridine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0020037	molecular_function	heme binding
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0020037	molecular_function	heme binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue 0PY A 501

Chain	Residue
A	PHE87
A	ALA264
A	MNH503

site_id	AC2
Number of Residues	12
Details	binding site for residue WAA A 502

Chain	Residue
A	GLN73
A	ALA74
A	MET185
A	LEU188
A	LEU437
A	HOH715
A	LEU20
A	VAL26
A	LEU29
A	ARG47
A	TYR51
A	SER72

site_id	AC3
Number of Residues	24
Details	binding site for residue MNH A 503

Chain	Residue
A	LYS69
A	LEU86
A	PHE87
A	TRP96
A	ILE153
A	ALA264
A	THR269
A	THR327
A	ALA328
A	PHE331
A	PRO392
A	GLY394
A	ARG398
A	ALA399
A	CYS400
A	ILE401
A	GLY402
A	0PY501
A	HOH630
A	HOH660
A	HOH706
A	HOH726
A	HOH728
A	HOH770

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 504

Chain	Residue
A	LYS391
A	GLY394
A	ASN395
A	GLY396
A	GLN403

site_id	AC5
Number of Residues	3
Details	binding site for residue 0PY C 501

Chain	Residue
C	PHE87
C	ALA264
C	MNH504

site_id	AC6
Number of Residues	7
Details	binding site for residue 0PY C 502

Chain	Residue
C	PHE158
C	TYR160
C	PHE162
C	HIS171
C	PHE173
C	LEU215
C	ILE219

site_id	AC7
Number of Residues	14
Details	binding site for residue WAA C 503

Chain	Residue
C	LEU20
C	PRO25
C	VAL26
C	LEU29
C	ALA44
C	ARG47
C	TYR51
C	SER72
C	GLN73
C	ALA74
C	LEU75
C	PHE87
C	LEU188
C	LEU437

site_id	AC8
Number of Residues	25
Details	binding site for residue MNH C 504

Chain	Residue
C	LYS69
C	LEU75
C	LEU86
C	PHE87
C	TRP96
C	ILE153
C	ALA264
C	THR269
C	THR327
C	ALA328
C	PHE331
C	PRO392
C	PHE393
C	GLY394
C	ARG398
C	ALA399
C	CYS400
C	ILE401
C	0PY501
C	HOH618
C	HOH633
C	HOH667
C	HOH672
C	HOH740
C	HOH780

site_id	AC9
Number of Residues	7
Details	binding site for residue GOL C 505

Chain	Residue
C	HOH691
C	TRP130
C	LEU133
C	ASN134
C	ALA448
C	SER450
C	LYS452

site_id	AD1
Number of Residues	4
Details	binding site for residue GOL C 506

Chain	Residue
C	ASP68
C	TYR334
C	LYS336
C	HOH699

site_id	AD2
Number of Residues	2
Details	binding site for residue GOL C 507

Chain	Residue
C	LYS9
C	HOH621

Functional Information from PROSITE/UniProt

site_id	PS00086
Number of Residues	10
Details	CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG

Chain	Residue	Details
A	PHE393-GLY402

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:15020590, ECO:0007744\|PDB:1SMJ

Chain	Residue	Details
A	TYR51
C	TYR51

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:10051560, ECO:0000269\|PubMed:11695889, ECO:0000269\|PubMed:11695892, ECO:0000269\|PubMed:14653735, ECO:0000269\|PubMed:15020590, ECO:0000269\|PubMed:15299332, ECO:0000269\|PubMed:16403573, ECO:0000269\|PubMed:17077084, ECO:0000269\|PubMed:17429965, ECO:0000269\|PubMed:17868686, ECO:0000269\|PubMed:18004886, ECO:0000269\|PubMed:18298086, ECO:0000269\|PubMed:18619466, ECO:0000269\|PubMed:18721129, ECO:0000269\|PubMed:19492389, ECO:0000269\|PubMed:20180779, ECO:0000269\|PubMed:20947800, ECO:0000269\|PubMed:21110374, ECO:0000269\|PubMed:21875028, ECO:0000269\|PubMed:7578081, ECO:0000269\|PubMed:8342039, ECO:0000269\|PubMed:9033595, ECO:0007744\|PDB:1BU7, ECO:0007744\|PDB:1BVY, ECO:0007744\|PDB:1FAG, ECO:0007744\|PDB:1FAH, ECO:0007744\|PDB:1JME, ECO:0007744\|PDB:1JPZ, ECO:0007744\|PDB:1P0V, ECO:0007744\|PDB:1P0W, ECO:0007744\|PDB:1P0X, ECO:0007744\|PDB:1SMI, ECO:0007744\|PDB:1SMJ, ECO:0007744\|PDB:1YQO, ECO:0007744\|PDB:1YQP, ECO:0007744\|PDB:1ZO4, ECO:0007744\|PDB:1ZO9, ECO:0007744\|PDB:1ZOA, ECO:0007744\|PDB:2BMH, ECO:0007744\|PDB:2HPD, ECO:0007744\|PDB:2IJ2, ECO:0007744\|PDB:2IJ3, ECO:0007744\|PDB:2IJ4, ECO:0007744\|PDB:2J1M, ECO:0007744\|PDB:2J4S, ECO:0007744\|PDB:2UWH, ECO:0007744\|PDB:3BEN, ECO:0007744\|PDB:3CBD, ECO:0007744\|PDB:3EKB, ECO:0007744\|PDB:3EKD, ECO:0007744\|PDB:3EKF, ECO:0007744\|PDB:3HF2, ECO:0007744\|PDB:3KX3, ECO:0007744\|PDB:3KX4, ECO:0007744\|PDB:3KX5, ECO:0007744\|PDB:3M4V, ECO:0007744\|PDB:3NPL

Chain	Residue	Details
A	CYS400
C	CYS400

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000305\|PubMed:16403573, ECO:0000305\|PubMed:7578081

Chain	Residue	Details
A	THR268
C	THR268

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
A	THR268	electrostatic stabiliser, steric role
A	PHE393	electrostatic stabiliser, steric role
A	CYS400	electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 699

Chain	Residue	Details
C	THR268	electrostatic stabiliser, steric role
C	PHE393	electrostatic stabiliser, steric role
C	CYS400	electrostatic stabiliser

224004

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