1BLL

X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004177	molecular_function	aminopeptidase activity
E	0004180	molecular_function	carboxypeptidase activity
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0016787	molecular_function	hydrolase activity
E	0016805	molecular_function	dipeptidase activity
E	0019538	biological_process	protein metabolic process
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
E	0070006	molecular_function	metalloaminopeptidase activity
E	0097718	molecular_function	disordered domain specific binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 488

Chain	Residue
E	ASP255
E	ASP332
E	GLU334
E	ZN489
I	L2O2

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN E 489

Chain	Residue
E	ZN488
I	L2O2
E	LYS250
E	ASP255
E	ASP273
E	GLU334

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR CHAIN I OF AMASTATIN

Chain	Residue
E	LYS250
E	ASP255
E	LYS262
E	MET270
E	ASP273
E	ASP332
E	GLU334
E	ARG336
E	THR359
E	LEU360
E	GLY362
E	ALA363
E	ILE366
E	ILE366
E	ARG425
E	GLY428
E	ZN488
E	ZN489
E	HOH594

---

Functional Information from PROSITE/UniProt

site_id	PS00631
Number of Residues	8
Details	CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL

Chain	Residue	Details
E	ASN330-LEU337

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:7578088

Chain	Residue	Details
E	ILE294
E	LEU368

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:7619821, ECO:0007744|PDB:1LCP

Chain	Residue	Details
E	ILE202
E	ARG203
E	LYS205
E	CYS303

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A

Chain	Residue	Details
E	SER282
E	ALA287
E	ASN305

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LCP

Chain	Residue	Details
E	LEU292

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:7578088, ECO:0000269|PubMed:7619821, ECO:0007744|PDB:1LAN, ECO:0007744|PDB:1LCP

Chain	Residue	Details
E	ILE294

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A

Chain	Residue	Details
E	MET364

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:17157838, ECO:0000269|PubMed:8506345, ECO:0007744|PDB:1BPM, ECO:0007744|PDB:2EWB, ECO:0007744|PDB:2J9A

Chain	Residue	Details
E	ILE366

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q68FS4

Chain	Residue	Details
E	SER42
E	PHE54

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPY7

Chain	Residue	Details
E	PRO45
E	PHE61
E	LEU103
E	ILE476

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CPY7

Chain	Residue	Details
E	PRO180

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P28838

Chain	Residue	Details
E	ALA194
E	PRO238

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPY7

Chain	Residue	Details
E	THR455

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 587

Chain	Residue	Details
E	ILE294	electrostatic stabiliser
E	LEU368	electrostatic stabiliser

---