5K4L

Crystal structure of KDM5A in complex with a naphthyridone inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
B	0003677	molecular_function	DNA binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue NI A 901

Chain	Residue
A	HIS483
A	GLU485
A	HIS571
A	6QN904

---

site_id	AC2
Number of Residues	3
Details	binding site for residue ZN A 902

Chain	Residue
A	CYS676
A	CYS679
A	CYS699

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 903

Chain	Residue
A	CYS692
A	CYS709
A	CYS690
A	SER691

---

site_id	AC4
Number of Residues	11
Details	binding site for residue 6QN A 904

Chain	Residue
A	TYR472
A	SER478
A	PHE480
A	HIS483
A	GLU485
A	ASN493
A	LYS501
A	TRP503
A	HIS571
A	ASN575
A	NI901

---

site_id	AC5
Number of Residues	4
Details	binding site for residue NI B 901

Chain	Residue
B	HIS483
B	GLU485
B	HIS571
B	6QN904

---

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN B 902

Chain	Residue
B	CYS676
B	ALA678
B	CYS679
B	CYS699
B	HIS702

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN B 903

Chain	Residue
B	CYS690
B	CYS692
B	CYS707
B	CYS709

---

site_id	AC8
Number of Residues	11
Details	binding site for residue 6QN B 904

Chain	Residue
B	TYR472
B	VAL473
B	SER479
B	PHE480
B	HIS483
B	ASN493
B	LYS501
B	TRP503
B	HIS571
B	ASN575
B	NI901

---

Functional Information from PROSITE/UniProt

site_id	PS01359
Number of Residues	45
Details	ZF_PHD_1 Zinc finger PHD-type signature. CmfCgrgnnedkl....................................LlCdg..Cdds.YHtfClipplpdvpkgd.................................WrCpkC

Chain	Residue	Details
A	CYS296-CYS340

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	100
Details	ZN_FING: PHD-type 1 => ECO:0000255|PROSITE-ProRule:PRU00146

Chain	Residue	Details
A	LEU293-GLU343
B	LEU293-GLU343

---

site_id	SWS_FT_FI2
Number of Residues	104
Details	ZN_FING: C5HC2 => ECO:0000269|PubMed:27214401, ECO:0000269|PubMed:27499454, ECO:0007744|PDB:5CEH

Chain	Residue	Details
A	CYS676-LEU728
B	CYS676-LEU728

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:26645689, ECO:0000269|PubMed:27427228

Chain	Residue	Details
A	TYR409
A	SER491
A	ASN493
A	LYS501
B	TYR409
B	SER491
B	ASN493
B	LYS501

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000305|PubMed:26645689, ECO:0000305|PubMed:27214401, ECO:0000305|PubMed:27427228, ECO:0000305|PubMed:27499454

Chain	Residue	Details
A	HIS483
A	HIS571
B	HIS483
B	HIS571

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:26645689, ECO:0000305|PubMed:27214401, ECO:0000305|PubMed:27427228, ECO:0000305|PubMed:27499454

Chain	Residue	Details
A	GLU485
B	GLU485

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER204
B	SER204

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS191
B	LYS191

---