6ZAL

Room temperature XFEL Isopenicillin N synthase structure in complex with Fe and ACV after exposure to dioxygen for 500ms without glycerol.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009058	biological_process	biosynthetic process
A	0016216	molecular_function	isopenicillin-N synthase activity
A	0016491	molecular_function	oxidoreductase activity
A	0017000	biological_process	antibiotic biosynthetic process
A	0031418	molecular_function	L-ascorbic acid binding
A	0042318	biological_process	penicillin biosynthetic process
A	0044283	biological_process	small molecule biosynthetic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue SO4 A 401

Chain	Residue
A	ARG37
A	LYS208
A	ARG300

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site_id	AC2
Number of Residues	17
Details	binding site for residue ACV A 402

Chain	Residue
A	HIS214
A	ASP216
A	SER281
A	PHE285
A	OXY403
A	FE2404
A	HOH509
A	HOH512
A	HOH582
A	HOH606
A	HOH617
A	ARG87
A	TYR91
A	SER183
A	ILE187
A	TYR189
A	PHE211

---

site_id	AC3
Number of Residues	5
Details	binding site for residue OXY A 403

Chain	Residue
A	HIS214
A	HIS270
A	ACV402
A	FE2404
A	HOH534

---

site_id	AC4
Number of Residues	6
Details	binding site for residue FE2 A 404

Chain	Residue
A	HIS214
A	ASP216
A	HIS270
A	ACV402
A	OXY403
A	HOH534

---

Functional Information from PROSITE/UniProt

site_id	PS00185
Number of Residues	10
Details	IPNS_1 Isopenicillin N synthase signature 1. KkAveSfCYL

Chain	Residue	Details
A	LYS97-LEU106

---

site_id	PS00186
Number of Residues	14
Details	IPNS_2 Isopenicillin N synthase signature 2. LInCGSymAhlTnN

Chain	Residue	Details
A	LEU250-ASN263

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS

Chain	Residue	Details
A	ARG87
A	TYR91
A	TYR189
A	ASP216
A	SER281

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS

Chain	Residue	Details
A	SER183

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE

Chain	Residue	Details
A	HIS214

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ, ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2, ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4, ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1, ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN, ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW, ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04, ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06, ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X, ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI, ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4, ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB, ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP, ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1, ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60, ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU, ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3

Chain	Residue	Details
A	HIS270

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805

Chain	Residue	Details
A	ARG279

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0007744|PDB:1QJE

Chain	Residue	Details
A	PHE211

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 145

Chain	Residue	Details
A	PHE211	polar/non-polar interaction, steric role
A	HIS214	metal ligand
A	ASP216	metal ligand
A	HIS270	metal ligand

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