6JVC

Structure of the Cobalt Protoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan

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	14
Details	binding site for residue WAA A 501

Chain	Residue
A	LEU20
A	PHE87
A	LEU188
A	MET354
A	LEU437
A	HOH772
A	VAL26
A	LEU29
A	ARG47
A	TYR51
A	SER72
A	GLN73
A	ALA74
A	LEU75

---

site_id	AC2
Number of Residues	4
Details	binding site for residue GOL A 502

Chain	Residue
A	ASP68
A	HIS92
A	LYS336
A	HOH608

---

site_id	AC3
Number of Residues	3
Details	binding site for residue GOL A 503

Chain	Residue
A	VAL286
A	GLU377
A	HOH701

---

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL A 504

Chain	Residue
A	LYS391
A	GLY394
A	ASN395
A	GLY396
A	ALA399
A	GLN403
A	HOH648
A	HOH687
A	HOH809

---

site_id	AC5
Number of Residues	2
Details	binding site for residue GOL A 505

Chain	Residue
A	ARG79
A	HOH709

---

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL A 506

Chain	Residue
A	LYS24
A	ALA28
A	LYS31
A	HOH818

---

site_id	AC7
Number of Residues	4
Details	binding site for residue GOL A 507

Chain	Residue
A	ASP121
A	ARG161
C	GLU131
C	ARG132

---

site_id	AC8
Number of Residues	8
Details	binding site for residue GOL A 508

Chain	Residue
A	TRP130
A	GLU131
A	LEU133
A	ASN134
A	ALA448
A	SER450
A	HOH631
A	HOH776

---

site_id	AC9
Number of Residues	7
Details	binding site for residue GOL A 509

Chain	Residue
A	ILE366
A	TRP367
A	ARG378
A	ALA384
A	ILE385
A	HOH693
A	HOH737

---

site_id	AD1
Number of Residues	6
Details	binding site for residue GOL A 510

Chain	Residue
A	GLN73
A	PHE77
A	ASP80
A	HOH682
A	HOH832
A	HOH840

---

site_id	AD2
Number of Residues	4
Details	binding site for residue GOL A 511

Chain	Residue
A	ASN319
A	PRO382
A	HOH604
A	HOH607

---

site_id	AD3
Number of Residues	29
Details	binding site for residue COH A 512

Chain	Residue
A	LYS69
A	LEU86
A	PHE87
A	TRP96
A	ILE153
A	ALA264
A	GLY265
A	THR268
A	THR269
A	LEU322
A	THR327
A	ALA328
A	PHE331
A	PRO392
A	PHE393
A	GLY394
A	ARG398
A	ALA399
A	CYS400
A	ILE401
A	GLY402
A	ALA406
A	DMS513
A	HOH654
A	HOH655
A	HOH656
A	HOH674
A	HOH727
A	HOH749

---

site_id	AD4
Number of Residues	3
Details	binding site for residue DMS A 513

Chain	Residue
A	PHE87
A	ALA264
A	COH512

---

site_id	AD5
Number of Residues	13
Details	binding site for residue WAA C 501

Chain	Residue
C	LEU29
C	ARG47
C	TYR51
C	SER72
C	GLN73
C	ALA74
C	LEU75
C	PHE87
C	LEU188
C	LEU437
C	HOH690
C	LEU20
C	VAL26

---

site_id	AD6
Number of Residues	5
Details	binding site for residue GOL C 502

Chain	Residue
C	ILE366
C	ARG378
C	ALA384
C	HOH651
C	HOH665

---

site_id	AD7
Number of Residues	6
Details	binding site for residue GOL C 503

Chain	Residue
C	ASP23
C	ASP182
C	MET185
C	ASN186
C	GLU435
C	THR436

---

site_id	AD8
Number of Residues	3
Details	binding site for residue GOL C 504

Chain	Residue
C	TRP90
C	HIS92
C	TYR334

---

site_id	AD9
Number of Residues	6
Details	binding site for residue GOL C 505

Chain	Residue
C	VAL178
C	LEU181
C	ASP182
C	GLU267
C	THR436
C	THR438

---

site_id	AE1
Number of Residues	5
Details	binding site for residue GOL C 506

Chain	Residue
C	LYS391
C	GLY394
C	ASN395
C	GLY396
C	GLN403

---

site_id	AE2
Number of Residues	4
Details	binding site for residue GOL C 507

Chain	Residue
C	ASP80
C	LYS187
C	GLN206
C	HOH742

---

site_id	AE3
Number of Residues	2
Details	binding site for residue GOL C 508

Chain	Residue
C	LYS9
C	HOH607

---

site_id	AE4
Number of Residues	4
Details	binding site for residue GOL C 509

Chain	Residue
C	LYS241
C	GLY246
C	HIS285
C	GLN288

---

site_id	AE5
Number of Residues	6
Details	binding site for residue GOL C 510

Chain	Residue
C	GLN288
C	ALA291
C	GLU292
C	LYS451
C	HOH749
C	HOH754

---

site_id	AE6
Number of Residues	7
Details	binding site for residue GOL C 511

Chain	Residue
C	ASP68
C	THR91
C	HIS92
C	TYR334
C	LYS336
C	GOL512
C	HOH602

---

site_id	AE7
Number of Residues	5
Details	binding site for residue GOL C 512

Chain	Residue
C	THR91
C	LYS97
C	GLN397
C	GOL511
C	HOH737

---

site_id	AE8
Number of Residues	2
Details	binding site for residue GOL C 513

Chain	Residue
C	ARG79
C	TYR256

---

site_id	AE9
Number of Residues	25
Details	binding site for residue COH C 514

Chain	Residue
C	LYS69
C	LEU86
C	PHE87
C	TRP96
C	ALA264
C	THR268
C	THR269
C	LEU322
C	THR327
C	PHE331
C	PRO392
C	PHE393
C	GLY394
C	ARG398
C	ALA399
C	CYS400
C	ILE401
C	PHE405
C	DMS515
C	HOH642
C	HOH650
C	HOH655
C	HOH730
C	HOH732
C	HOH744

---

site_id	AF1
Number of Residues	3
Details	binding site for residue DMS C 515

Chain	Residue
C	PHE87
C	ALA264
C	COH514

---

site_id	AF2
Number of Residues	7
Details	binding site for residue TRS C 516

Chain	Residue
C	TRP130
C	LEU133
C	ASN134
C	ALA448
C	LYS449
C	SER450
C	LYS452

---

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

---