5KKN

Crystal structure of human ACC2 BC domain in complex with ND-646, the primary amide of ND-630

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0003989	molecular_function	acetyl-CoA carboxylase activity
B	0005524	molecular_function	ATP binding
B	0046872	molecular_function	metal ion binding
C	0003989	molecular_function	acetyl-CoA carboxylase activity
C	0005524	molecular_function	ATP binding
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue 6U3 B 801

Chain	Residue
B	ILE270
B	VAL680
B	TRP681
B	PHE704
B	LYS274
B	ARG277
B	ARG281
B	VAL587
B	PRO590
B	GLU593
B	LYS678
B	ASN679

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site_id	AC2
Number of Residues	10
Details	binding site for residue 6U3 C 801

Chain	Residue
C	ILE270
C	LYS274
C	ARG277
C	ARG281
C	VAL587
C	PRO590
C	GLU593
C	MET594
C	TRP681
C	PHE704

---

Functional Information from PROSITE/UniProt

site_id	PS00866
Number of Residues	15
Details	CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. FPLMIKASeggGGkG

Chain	Residue	Details
B	PHE449-GLY463

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site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL

Chain	Residue	Details
B	PHE578-LEU585

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409

Chain	Residue	Details
B	GLU660
C	GLU660

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
B	ALA272
C	ALA272

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
B	ILE293
B	VAL297
B	TRP402
B	GLU671
C	ILE293
C	VAL297
C	TRP402
C	GLU671

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q13085

Chain	Residue	Details
B	PHE371
B	GLU377
B	THR394
B	VAL397
C	PHE371
C	GLU377
C	THR394
C	VAL397

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:E9Q4Z2

Chain	Residue	Details
B	VAL409
C	VAL409

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11497

Chain	Residue	Details
B	ILE422
C	ILE422

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine; by AMPK => ECO:0000269|PubMed:12488245, ECO:0000269|PubMed:19900410

Chain	Residue	Details
B	VAL424
C	VAL424

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