Structure of PDB 4h1q Chain A

Receptor sequence

>4h1qA (length=160) Species: 9606 (Homo sapiens)

FEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRV
YSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDEL
WSLGKGQGYSLFLVAAHQFGHALGLDHSSVPEALMYPMYRFTEGPPLHKD
DVNGIRHLYG

3D structure

• PDB: 4h1q Crystallization of bi-functional ligand protein complexes.
• Chain: A
• Resolution: 1.59 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H226 Q227 H230 H236
• Catalytic site (residue number reindexed from 1): H117 Q118 H121 H127
• Enzyme Commision number: 3.4.24.35: gelatinase B.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	H226 H230 H236	H117 H121 H127
BS02	ZN	A	H175 D177 H190 H203	H66 D68 H81 H94
BS03	CA	A	D165 G197 Q199 D201	D56 G88 Q90 D92
BS04	CA	A	D131 D206 E208	D22 D97 E99
BS05	CA	A	D182 G183 D185 L187 D205 E208	D73 G74 D76 L78 D96 E99
BS06	CA	A	S149 T152 L154	S40 T43 L45
BS07	0XX	A	Y179 P180 F181 D182 L187 L188 A189 H190 A191 F192 L222 H226 Q227 H230 H236 L243 Y245 P246 M247 Y248	Y70 P71 F72 D73 L78 L79 A80 H81 A82 F83 L113 H117 Q118 H121 H127 L134 Y136 P137 M138 Y139
BS08	0XX	A	Y245 P246	Y136 P137

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity
• GO:0008237 metallopeptidase activity
• GO:0008270 zinc ion binding

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0031012 extracellular matrix

External links

• PDB: RCSB:4h1q, PDBe:4h1q, PDBj:4h1q
• PDBsum: 4h1q
• PubMed: 23567804
• UniProt: P14780|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)