5APA

Crystal structure of human aspartate beta-hydroxylase isoform a

Replaces:  3RCQ

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0018193	biological_process	peptidyl-amino acid modification
A	0042264	biological_process	peptidyl-aspartic acid hydroxylation
A	0062101	molecular_function	peptidyl-aspartic acid 3-dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NI A 1759

Chain	Residue
A	HIS679
A	HIS725
A	LMR1760
A	HOH2056
A	HOH2088

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LMR A 1760

Chain	Residue
A	ARG688
A	HIS690
A	HIS725
A	ARG735
A	ILE737
A	ILE739
A	NI1759
A	HOH2055
A	HOH2056
A	TRP625
A	SER668
A	MET670
A	HIS679

---

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 1761

Chain	Residue
A	SER722

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human aspartate beta-hydroxylase isoform A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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